Danish
Uniprot ID:  A0A891LWT6
  • Protein: Putative cytochrome P450
  • Organism: Planomonospora sp
  • Length: 378
  • Sequence:
    • MFTPLAPEMLRDPYPRYAELRREAPVQWFEPLRAWLVLRHADCTRVVTDSTTFSNDLAVLGEEPPTAILGLQNLDPPEHTSVRHALVRALKSVDVGIWARESAAHAERLLADADLNGFDFVSEFAEPLSAESMRILFGVPDFGAPDEFHAAQRALVLSMDAGLEPERGAPGVRARDHLSGVLEPWVMRPPKNGLLSGIDIASAGRLRRYLVNSLRQILVAGFSSSSSMLGLALKTLAEQGLLDRDEPLAVTPTAYNEVVRHSGAVQVDSRACAQDVELGGRLIRRGDEVVAVIAAANRDPDVFERPDDLVVDRSPNPHLGFGRGVHSCLGTALATALHARVLTTLSERYRVRLDGTPVMRPTATLHGLDRLPVVLLPR
Exclude chains with
Mutations (vs. UniProt)
Clear
Number of chains:  3
PDB ID:  pdb_00009jv0 , Chain A 
Resolution 1.90 Å
Residue indices (Uniprot), coverage 1-378 (1-378), 1.00
Difference from Uniprot sequence expression tag:initiating methionine
Mutations (UniProt numbering) None
Insertions 0insMGSSHHHHHHSSGLVPRGSH
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id A
Missing residues 58ALA-64PRO:188ARG-188ARG:202SER-203ALA
Structural gaps Exists
label_asym_ids of heme B
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.09 Å
PDB ID:  pdb_00009jvf , Chain A 
Resolution 1.90 Å
Residue indices (Uniprot), coverage 1-378 (1-378), 1.00
Difference from Uniprot sequence expression tag:initiating methionine
Mutations (UniProt numbering) None
Insertions 0insMGSSHHHHHHSSGLVPRGSH
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id A
Missing residues 188ARG-188ARG:197GLY-205ARG
Structural gaps Exists
label_asym_ids of heme C
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å
PDB ID:  pdb_00009jvj , Chain A 
Resolution 2.00 Å
Residue indices (Uniprot), coverage 1-378 (1-378), 1.00
Difference from Uniprot sequence engineered mutation:expression tag:initiating methionine
Mutations (UniProt numbering) V219H
Insertions 0insMGSSHHHHHHSSGLVPRGSH
Deletions None
Sequence identity to UniProt 0.9974
auth_asym_id A
Missing residues 188ARG-188ARG:199ASP-205ARG
Structural gaps Exists
label_asym_ids of heme C
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.10 Å