Danish
Uniprot ID:  P9WPP9
  • Protein: Sterol 14alpha-demethylase
  • Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
  • Length: 451
  • Sequence:
    • MSAVALPRVSGGHDEHGHLEEFRTDPIGLMQRVRDECGDVGTFQLAGKQVVLLSGSHANEFFFRAGDDDLDQAKAYPFMTPIFGEGVVFDASPERRKEMLHNAALRGEQMKGHAATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSACLIGKKFRDQLDGRFAKLYHELERGTDPLAYVDPYLPIESFRRRDEARNGLVALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPESYRNDHSKMVVQLAQPACVRYRRRTGV
Exclude chains with
Mutations (vs. UniProt)
Clear
Number of chains:  13
PDB ID:  pdb_00002cib , Chain A 
Resolution 1.50 Å
Residue indices (Uniprot), coverage 5-448 (1-451), 1.00
Difference from Uniprot sequence engineered mutation
Mutations (UniProt numbering) C37L, C442A
Insertions 451insHHHH
Deletions None
Sequence identity to UniProt 0.9956
auth_asym_id A
Structural gaps Exists
label_asym_ids of heme B
Available structure PDB
PDB ID:  pdb_00002ci0 , Chain A 
Resolution 1.53 Å
Residue indices (Uniprot), coverage 3-448 (1-451), 1.00
Difference from Uniprot sequence engineered mutation
Mutations (UniProt numbering) C37L, C442A
Insertions 451insHHHH
Deletions None
Sequence identity to UniProt 0.9956
auth_asym_id A
Structural gaps Exists
label_asym_ids of heme B
Available structure PDB
PDB ID:  pdb_00001x8v , Chain A 
Resolution 1.55 Å
Residue indices (Uniprot), coverage 2-449 (1-451), 1.00
Difference from Uniprot sequence engineered mutation:expression tag
Mutations (UniProt numbering) C37L, C442A
Insertions 451insHHHH
Deletions None
Sequence identity to UniProt 0.9956
auth_asym_id A
Missing residues 85GLU-94GLU:217PRO-222ASP:235GLU-237GLY
Structural gaps Exists
label_asym_ids of heme B
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.10 Å
PDB ID:  pdb_00002w0b , Chain A 
Resolution 1.56 Å
Residue indices (Uniprot), coverage 3-449 (1-451), 1.00
Difference from Uniprot sequence engineered mutation
Mutations (UniProt numbering) C37L, C442A
Insertions 451insHHHH
Deletions None
Sequence identity to UniProt 0.9956
auth_asym_id A
Missing residues 216PRO-222ASP
Structural gaps Exists
label_asym_ids of heme B
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.10 Å
PDB ID:  pdb_00002w09 , Chain A 
Resolution 1.57 Å
Residue indices (Uniprot), coverage 4-449 (1-451), 1.00
Difference from Uniprot sequence engineered mutation
Mutations (UniProt numbering) C37L, C442A
Insertions 451insHHHH
Deletions None
Sequence identity to UniProt 0.9956
auth_asym_id A
Missing residues 85GLU-100LEU:217PRO-222ASP:235GLU-237GLY
Structural gaps Exists
label_asym_ids of heme B
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å
PDB ID:  pdb_00002w0a , Chain A 
Resolution 1.60 Å
Residue indices (Uniprot), coverage 3-449 (1-451), 1.00
Difference from Uniprot sequence conflict:engineered mutation
Mutations (UniProt numbering) C37L, G86A, C442A
Insertions 451insHHHH
Deletions None
Sequence identity to UniProt 0.9933
auth_asym_id A
Missing residues 90ASP-105LEU:217PRO-221SER:235GLU-236THR
Structural gaps Exists
label_asym_ids of heme B
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
PDB ID:  pdb_00002vku , Chain A 
Resolution 1.95 Å
Residue indices (Uniprot), coverage 6-449 (1-451), 1.00
Difference from Uniprot sequence engineered mutation
Mutations (UniProt numbering) C37L, C442A
Insertions 451insHHHH
Deletions None
Sequence identity to UniProt 0.9956
auth_asym_id A
label_asym_ids of heme F
Available structure PDB
PDB ID:  pdb_00001u13 , Chain A 
Resolution 2.01 Å
Residue indices (Uniprot), coverage 2-449 (1-451), 1.00
Difference from Uniprot sequence engineered mutation:expression tag
Mutations (UniProt numbering) C37L, C151T, C442A
Insertions 451insHHHH
Deletions None
Sequence identity to UniProt 0.9933
auth_asym_id A
Missing residues 85GLU-94GLU:217PRO-221SER
Structural gaps Exists
label_asym_ids of heme B
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.11 Å
PDB ID:  pdb_00001h5z , Chain A 
Resolution 2.05 Å
Residue indices (Uniprot), coverage 2-449 (1-451), 1.00
Mutations (UniProt numbering) None
Insertions 451insHHHH
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id A
Missing residues 91ALA-100LEU:219ASP-222ASP
Structural gaps Exists
label_asym_ids of heme B
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
PDB ID:  pdb_00001e9x , Chain A 
Resolution 2.10 Å
Residue indices (Uniprot), coverage 1-449 (1-451), 1.00
Mutations (UniProt numbering) None
Insertions 451insHHHH
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id A
label_asym_ids of heme B
Available structure PDB
PDB ID:  pdb_00001ea1 , Chain A 
Resolution 2.21 Å
Residue indices (Uniprot), coverage 3-449 (1-451), 1.00
Mutations (UniProt numbering) None
Insertions 451insHHHH
Deletions None
Sequence identity to UniProt 1.0000
auth_asym_id A
label_asym_ids of heme B
Available structure PDB
PDB ID:  pdb_00002bz9 , Chain A 
Resolution 2.21 Å
Residue indices (Uniprot), coverage 2-448 (1-451), 1.00
Difference from Uniprot sequence engineered mutation
Mutations (UniProt numbering) C37L, C442A
Insertions 451insHHHH
Deletions None
Sequence identity to UniProt 0.9956
auth_asym_id A
Missing residues 85GLU-98GLU:217PRO-220LYS
Structural gaps Exists
label_asym_ids of heme C
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.12 Å
PDB ID:  pdb_00002bz9 , Chain B 
Resolution 2.21 Å
Residue indices (Uniprot), coverage 2-448 (1-451), 1.00
Difference from Uniprot sequence engineered mutation
Mutations (UniProt numbering) C37L, C442A
Insertions 451insHHHH
Deletions None
Sequence identity to UniProt 0.9956
auth_asym_id B
Missing residues 85GLU-94GLU:217PRO-221SER
Structural gaps Exists
label_asym_ids of heme D
Available structure PDB and Modeled
RMSD of experimental residues after energy minimization 0.13 Å