Danish
Uniprot ID:  Q8KLL9
  • Protein: StaH
  • Organism: Streptomyces toyocaensis
  • Length: 398
  • Sequence:
    • MSGDDRPPIHTLRQGFDPADELRAAGELTRVRLGSGADAEHTWLATGHDVVRQVLGDHTRFSTRRRFDRNDEIGGKGVFRPRELVGNLMDYDPPEHTRLRRLLAPGFTHRKIRRMAPYIEQIVTERLDEMEREGSPADLIELFADEVPGPVLCELLGVPRDDRAMFLQLCHRHLDASLSGRRRAAAGEAFSRYLVTMVARERKDPGDGLIGMVVAEHGDTVTDEELRGVCVQMMLAGDDNISGMIGLGVLALLRNPEQIAALRGDVPAAERAVDELIRYLTVPYAPTPRTAIEDSTVGDQVIKAGETVLCSLPTANRDPALLPDADRLDVTREAVPHVAFGHGVHHCLGAALARLELRIAYTALWRRFPDLRLADPDGATEFRLSTPAYGISRLMVTW
Exclude chains with
Mutations (vs. UniProt)
Clear
Number of chains:  3
PDB ID:  pdb_00005ex6 , Chain A 
Resolution 2.40 Å
Residue indices (Uniprot), coverage 6-398 (1-398), 1.00
Difference from Uniprot sequence expression tag:initiating methionine
Mutations (UniProt numbering) None
Insertions 0insMGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSEF
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id C
Missing residues 35SER-38ASP:70ASN-70ASN
Structural gaps Exists
label_asym_ids of heme E
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.10 Å
PDB ID:  pdb_00005ex6 , Chain B 
Resolution 2.40 Å
Residue indices (Uniprot), coverage 6-398 (1-398), 1.00
Difference from Uniprot sequence expression tag:initiating methionine
Mutations (UniProt numbering) None
Insertions 0insMGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSEF
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id A
Missing residues 35SER-39ALA:70ASN-71ASP
Structural gaps Exists
label_asym_ids of heme I
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å
PDB ID:  pdb_00005ex6 , Chain C 
Resolution 2.40 Å
Residue indices (Uniprot), coverage 6-398 (1-398), 1.00
Difference from Uniprot sequence expression tag:initiating methionine
Mutations (UniProt numbering) None
Insertions 0insMGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSEF
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id B
Missing residues 34GLY-39ALA:68ASP-83GLU
Structural gaps Exists
label_asym_ids of heme L
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å