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Uniprot ID: A0A6I8WFM0

Protein: Catalase
Organism: Escherichia coli M8
Length: 750
Sequence:

MIKKNKADFTSNGSNNKAISTVEPHYEDTAPAEKVIKSLTSISPPGVEPMMPGSDKTPKNRNEKLTQLDKFRFAPQGESLRTNQGVKISDNQNSLKSGARGSTLLEDFILREKITHFDHERIPERVVHARGTGAHGYFQVYESLASYTTAEFLQDPSVKTPVFVRFSTVQGSRGSADTVRDIRGWATKFYTKEGTFDLVGNNTPVFFIQDAIKFPDFVHAVKPEPHNEIPQGQSAHDTFWDYISLQPETLHNVMWVMSDRGIPRSYRMMEGFGIHTYKMINAEGQCHFIRFHWKPVYGVSSLIWDEAQLLTGCDPDFHRRELWESIEAGDYPEYELGLQIIPEEDEHKFDFDILDPTKLIPESLVPVHLVGKMVLNRNPDNYFSETEQVAFCPGNIVPGIDFSDDPLLQGRLFSYIDTQISRLGGVNFHEIPINKPICPFHNHQRDGMHRMSISGTANYEPNSINNNWPREAPPTEGGFTTYPQPVNGYKSRKRSSTFIDFYSQPRLFWLSQTKVEQNHIVGGFSFELGKVVRPWIRERVVNQLTYIDHQLAQSVADNLGIKLSQEQLKHPLPGPINGLSKDRSLSMYDGHHQILKSRQVAILAADGVCGDAIDNIMKTLKKYGVHGKIFAPHVGRITSLQGNEIEVNGTIEGNPSVMVDAVIIPDGEDSIDSLMKNGNAKHYVIQAFKHLKAIGLQGKAFKLYDALPLPKPDEGIVVGDKAADLAEAFCNVMRGHRIWSRESVAQEIAG

Number of chains: 12

PDB ID: pdb_00006lfk , Chain A
Resolution	2.10 Å
Residue indices (Uniprot), coverage	16-750 (1-750), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	A
Missing residues	31PRO-46GLY
Structural gaps	Exists
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00006lfk , Chain B
Resolution	2.10 Å
Residue indices (Uniprot), coverage	16-750 (1-750), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	B
Missing residues	33GLU-46GLY
Structural gaps	Exists
label_asym_ids of heme	F
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00006lfk , Chain C
Resolution	2.10 Å
Residue indices (Uniprot), coverage	16-750 (1-750), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	C
Missing residues	35VAL-46GLY
Structural gaps	Exists
label_asym_ids of heme	G
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.15 Å

PDB ID: pdb_00006lfk , Chain D
Resolution	2.10 Å
Residue indices (Uniprot), coverage	16-750 (1-750), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	D
Missing residues	33GLU-47VAL
Structural gaps	Exists
label_asym_ids of heme	H
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00008j4q , Chain A
Resolution	2.10 Å
Residue indices (Uniprot), coverage	16-750 (1-750), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	A
Missing residues	33GLU-46GLY:609CYS-609CYS
Structural gaps	Exists
Nonstandard amino acids	OCS
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00008j4q , Chain B
Resolution	2.10 Å
Residue indices (Uniprot), coverage	16-750 (1-750), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	B
Missing residues	35VAL-46GLY:609CYS-609CYS
Structural gaps	Exists
Nonstandard amino acids	CSD
label_asym_ids of heme	F
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.19 Å

PDB ID: pdb_00008j4q , Chain C
Resolution	2.10 Å
Residue indices (Uniprot), coverage	16-750 (1-750), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	C
Missing residues	35VAL-46GLY:609CYS-609CYS
Structural gaps	Exists
Nonstandard amino acids	CSD
label_asym_ids of heme	G
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00008j4q , Chain D
Resolution	2.10 Å
Residue indices (Uniprot), coverage	16-750 (1-750), 1.00
Mutations (UniProt numbering)	None
Insertions	None
Deletions	None
Sequence identity to UniProt	1.0000
auth_asym_id	D
Missing residues	36ILE-46GLY:609CYS-609CYS
Structural gaps	Exists
Nonstandard amino acids	CSD
label_asym_ids of heme	H
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.18 Å

PDB ID: pdb_00008j4r , Chain A
Resolution	2.50 Å
Residue indices (Uniprot), coverage	16-750 (1-750), 1.00
Difference from Uniprot sequence	engineered mutation
Mutations (UniProt numbering)	F413Y
Insertions	None
Deletions	None
Sequence identity to UniProt	0.9987
auth_asym_id	A
Missing residues	33GLU-45PRO:609CYS-609CYS
Structural gaps	Exists
Nonstandard amino acids	CSD
label_asym_ids of heme	E
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.10 Å

PDB ID: pdb_00008j4r , Chain B
Resolution	2.50 Å
Residue indices (Uniprot), coverage	16-750 (1-750), 1.00
Difference from Uniprot sequence	engineered mutation
Mutations (UniProt numbering)	F413Y
Insertions	None
Deletions	None
Sequence identity to UniProt	0.9987
auth_asym_id	B
Missing residues	33GLU-46GLY:609CYS-609CYS
Structural gaps	Exists
Nonstandard amino acids	OCS
label_asym_ids of heme	F
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.12 Å

PDB ID: pdb_00008j4r , Chain C
Resolution	2.50 Å
Residue indices (Uniprot), coverage	15-750 (1-750), 1.00
Difference from Uniprot sequence	engineered mutation
Mutations (UniProt numbering)	F413Y
Insertions	None
Deletions	None
Sequence identity to UniProt	0.9987
auth_asym_id	C
Missing residues	33GLU-46GLY:609CYS-609CYS
Structural gaps	Exists
Nonstandard amino acids	OCS
label_asym_ids of heme	G
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.11 Å

PDB ID: pdb_00008j4r , Chain D
Resolution	2.50 Å
Residue indices (Uniprot), coverage	15-750 (1-750), 1.00
Difference from Uniprot sequence	engineered mutation
Mutations (UniProt numbering)	F413Y
Insertions	None
Deletions	None
Sequence identity to UniProt	0.9987
auth_asym_id	D
Missing residues	34LYS-46GLY:609CYS-609CYS
Structural gaps	Exists
Nonstandard amino acids	CSD
label_asym_ids of heme	H
Available structure	PDB and Modeled
RMSD of experimental residues after energy minimization	0.13 Å