Danish
Uniprot ID:  P15538
  • Protein: Cytochrome P450 11B1, mitochondrial
  • Organism: Human (Homo sapiens)
  • Length: 503
  • Sequence:
    • MALRAKAEVCMAVPWLSLQRAQALGTRAARVPRTVLPFEAMPRRPGNRWLRLLQIWREQGYEDLHLEVHQTFQELGPIFRYDLGGAGMVCVMLPEDVEKLQQVDSLHPHRMSLEPWVAYRQHRGHKCGVFLLNGPEWRFNRLRLNPEVLSPNAVQRFLPMVDAVARDFSQALKKKVLQNARGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFMPRSLSRWTSPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFSRPQQYTSIVAELLLNAELSPDAIKANSMELTAGSVDTTVFPLLMTLFELARNPNVQQALRQESLAAAASISEHPQKATTELPLLRAALKETLRLYPVGLFLERVASSDLVLQNYHIPAGTLVRVFLYSLGRNPALFPRPERYNPQRWLDIRGSGRNFYHVPFGFGMRQCLGRRLAEAEMLLLLHHVLKHLQVETLTQEDIKMVYSFILRPSMFPLLTFRAIN
Exclude chains with
Mutations (vs. UniProt)
Clear
Number of chains:  3
PDB ID:  pdb_00007e7f , Chain A 
Resolution 1.40 Å
Residue indices (Uniprot), coverage 31-502 (28-503), 0.95
Difference from Uniprot sequence engineered mutation:expression tag:initiating methionine
Mutations (UniProt numbering) R27K, W49R, L50N, L53N, W56R, L244N, W247N
Insertions 503insHHHHHH
Deletions L3-G25
Sequence identity to UniProt 0.9854
auth_asym_id A
label_asym_ids of heme B
Available structure PDB
PDB ID:  pdb_00006m7x , Chain A 
Resolution 2.10 Å
Residue indices (Uniprot), coverage 34-502 (31-503), 0.95
Difference from Uniprot sequence expression tag
Mutations (UniProt numbering) T26K, R27K, A28T, A29S, R30S
Insertions 503insHHHH
Deletions L3-G25
Sequence identity to UniProt 0.9896
auth_asym_id A
Missing residues 281SER-286TYR
Structural gaps Exists
label_asym_ids of heme D
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.09 Å
PDB ID:  pdb_00006m7x , Chain B 
Resolution 2.10 Å
Residue indices (Uniprot), coverage 34-502 (31-503), 0.95
Difference from Uniprot sequence expression tag
Mutations (UniProt numbering) T26K, R27K, A28T, A29S, R30S
Insertions 503insHHHH
Deletions L3-G25
Sequence identity to UniProt 0.9896
auth_asym_id B
Missing residues 281SER-285GLN:433GLY-435GLY
Structural gaps Exists
label_asym_ids of heme F
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.10 Å