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1H4I

Methylobacterium extorquens methanol dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005509molecular_functioncalcium ion binding
A0005886cellular_componentplasma membrane
A0015945biological_processmethanol metabolic process
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
A0052933molecular_functionalcohol dehydrogenase (cytochrome c(L)) activity
A0070968molecular_functionpyrroloquinoline quinone binding
B0004022molecular_functionalcohol dehydrogenase (NAD+) activity
B0015945biological_processmethanol metabolic process
B0015946biological_processmethanol oxidation
B0016491molecular_functionoxidoreductase activity
B0042597cellular_componentperiplasmic space
B0052933molecular_functionalcohol dehydrogenase (cytochrome c(L)) activity
C0003824molecular_functioncatalytic activity
C0005509molecular_functioncalcium ion binding
C0005886cellular_componentplasma membrane
C0015945biological_processmethanol metabolic process
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
C0030288cellular_componentouter membrane-bounded periplasmic space
C0046872molecular_functionmetal ion binding
C0052933molecular_functionalcohol dehydrogenase (cytochrome c(L)) activity
C0070968molecular_functionpyrroloquinoline quinone binding
D0004022molecular_functionalcohol dehydrogenase (NAD+) activity
D0015945biological_processmethanol metabolic process
D0015946biological_processmethanol oxidation
D0016491molecular_functionoxidoreductase activity
D0042597cellular_componentperiplasmic space
D0052933molecular_functionalcohol dehydrogenase (cytochrome c(L)) activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 701
ChainResidue
AGLU177
AASN261
AASP303
APQQ601

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 701
ChainResidue
CGLU177
CASN261
CASP303
CPQQ601

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PQQ A 601
ChainResidue
AVAL107
AARG109
ATHR159
ASER174
AGLY175
AALA176
AGLU177
ATHR241
ATRP243
AASN261
AARG331
AASN394
ATRP476
AGLY539
ATRP540
ACA701
AGLU55

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PQQ C 601
ChainResidue
CGLU55
CVAL107
CARG109
CTHR159
CSER174
CGLY175
CALA176
CGLU177
CTHR241
CTRP243
CASN261
CARG331
CASN394
CTRP476
CGLY539
CTRP540
CCA701

Functional Information from PROSITE/UniProt
site_idPS00363
Number of Residues29
DetailsBACTERIAL_PQQ_1 Bacterial quinoprotein dehydrogenases signature 1. NWvmpGKnydsnnFSdlkqINkgNVkqLR
ChainResidueDetails
AASN13-ARG41

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues60
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues22
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

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
CASP303

238895

PDB entries from 2025-07-16

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