Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2D0V

Crystal structure of methanol dehydrogenase from Hyphomicrobium denitrificans

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0030288cellular_componentouter membrane-bounded periplasmic space
A0046872molecular_functionmetal ion binding
B0004022molecular_functionalcohol dehydrogenase (NAD+) activity
B0015945biological_processmethanol metabolic process
B0015946biological_processmethanol oxidation
B0016491molecular_functionoxidoreductase activity
B0052933molecular_functionalcohol dehydrogenase (cytochrome c(L)) activity
D0005509molecular_functioncalcium ion binding
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
D0030288cellular_componentouter membrane-bounded periplasmic space
D0046872molecular_functionmetal ion binding
E0004022molecular_functionalcohol dehydrogenase (NAD+) activity
E0015945biological_processmethanol metabolic process
E0015946biological_processmethanol oxidation
E0016491molecular_functionoxidoreductase activity
E0052933molecular_functionalcohol dehydrogenase (cytochrome c(L)) activity
I0005509molecular_functioncalcium ion binding
I0016020cellular_componentmembrane
I0016491molecular_functionoxidoreductase activity
I0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
I0030288cellular_componentouter membrane-bounded periplasmic space
I0046872molecular_functionmetal ion binding
J0004022molecular_functionalcohol dehydrogenase (NAD+) activity
J0015945biological_processmethanol metabolic process
J0015946biological_processmethanol oxidation
J0016491molecular_functionoxidoreductase activity
J0052933molecular_functionalcohol dehydrogenase (cytochrome c(L)) activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 775
ChainResidue
AGLU177
AASN261
AASP303
APQQ601

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA D 775
ChainResidue
DGLU177
DASN261
DASP303
DPQQ601

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA I 775
ChainResidue
IASN261
IPQQ601
IGLU177

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE PQQ A 601
ChainResidue
AGLU55
AARG109
ATHR159
ASER174
AGLY175
AALA176
AGLU177
ATHR241
ATRP243
AASP303
AARG331
AASN394
AGLN395
ATRP476
AGLY539
ATRP540
APRO541
ACA775
AHOH810

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE PQQ D 601
ChainResidue
DGLU55
DARG109
DTHR159
DSER174
DGLY175
DALA176
DGLU177
DTHR241
DTRP243
DASN261
DASP303
DARG331
DASN394
DGLN395
DTRP476
DGLY539
DTRP540
DPRO541
DCA775
DHOH788

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE PQQ I 601
ChainResidue
IGLU55
ICYS104
IARG109
ITHR159
ISER174
IGLY175
IALA176
IGLU177
ITHR241
ITRP243
IASP303
IARG331
IASN394
IGLN395
ITRP476
IGLY539
ITRP540
ICA775
IHOH926

Functional Information from PROSITE/UniProt
site_idPS00363
Number of Residues29
DetailsBACTERIAL_PQQ_1 Bacterial quinoprotein dehydrogenases signature 1. NWvmpGKnydsnnYStstqINvdNVkqLK
ChainResidueDetails
AASN13-LYS41

site_idPS00364
Number of Residues22
DetailsBACTERIAL_PQQ_2 Bacterial quinoprotein dehydrogenases signature 2. WgwyaYDpaaNLIYYgsGnpAP
ChainResidueDetails
ATRP243-PRO264

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g72
ChainResidueDetails
AASP303

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g72
ChainResidueDetails
DASP303

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g72
ChainResidueDetails
IASP303

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon