Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3KP9

Structure of a bacterial homolog of vitamin K epoxide reductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0048038molecular_functionquinone binding
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE U10 A 501
ChainResidue
AVAL59
APHE114
AMET118
ALEU126
ACYS133
ATHR170
AARG63
ATRP64
AALA65
ATHR72
AALA73
AVAL75
AGLY76
AMET111

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG A 601
ChainResidue
ACYS212
ATYR228

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE HG A 602
ChainResidue
AHIS195

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues41
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AMET1-ARG20
AVAL88-PRO102
AGLY150-LYS158

site_idSWS_FT_FI2
Number of Residues100
DetailsTRANSMEM: Helical
ChainResidueDetails
ALEU21-LYS41
APHE67-ALA87
AALA103-VAL123
APHE129-LEU149
ALEU159-ALA179

site_idSWS_FT_FI3
Number of Residues131
DetailsTOPO_DOM: Periplasmic
ChainResidueDetails
ALEU42-GLU66
AALA124-GLN128
AASN180-ARG283

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AVAL59
AMET111

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Important for the reduction of the redox-active Cys-130 and Cys-133
ChainResidueDetails
ACYS50
ASER56
ACYS209
ACYS212

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon