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2AD7

crystal structure of methanol dehydrogenase from M. W3A1 (form C) in the presence of methanol

Functional Information from GO Data
ChainGOidnamespacecontents
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
B0004022molecular_functionalcohol dehydrogenase (NAD+) activity
B0005886cellular_componentplasma membrane
B0015945biological_processmethanol metabolic process
B0015946biological_processmethanol oxidation
B0016491molecular_functionoxidoreductase activity
B0052933molecular_functionalcohol dehydrogenase (cytochrome c(L)) 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
D0004022molecular_functionalcohol dehydrogenase (NAD+) activity
D0005886cellular_componentplasma membrane
D0015945biological_processmethanol metabolic process
D0015946biological_processmethanol oxidation
D0016491molecular_functionoxidoreductase activity
D0052933molecular_functionalcohol dehydrogenase (cytochrome c(L)) activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 702
ChainResidue
AGLU171
AASN255
AASP297
APQQ701

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 704
ChainResidue
CGLU171
CASN255
CASP297
CPQQ703

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE PQQ A 701
ChainResidue
ACYS103
ACYS104
AVAL107
AARG109
ATHR153
ASER168
AGLY169
AALA170
AGLU171
ATHR235
ATRP237
AASN255
AARG324
AASN387
ATRP467
AGLY530
ATRP531
ACA702
AHOH1822
AHOH1948
AHOH2338
AHOH4001
AGLU55

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE PQQ C 703
ChainResidue
CGLU55
CCYS103
CCYS104
CVAL107
CARG109
CTHR153
CSER168
CGLY169
CALA170
CGLU171
CTHR235
CTRP237
CASN255
CARG324
CASN387
CTRP467
CGLY530
CTRP531
CCA704
CHOH1851
CHOH1925
CHOH2005
CHOH4002

Functional Information from PROSITE/UniProt
site_idPS00364
Number of Residues22
DetailsBACTERIAL_PQQ_2 Bacterial quinoprotein dehydrogenases signature 2. WgwyaYDpklNLFYYgsGnpAP
ChainResidueDetails
ATRP237-PRO258

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP297
CASP297

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AGLU171
AASN255
CGLU171
CASN255

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g72
ChainResidueDetails
AASP297

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1g72
ChainResidueDetails
CASP297

site_idMCSA1
Number of Residues3
DetailsM-CSA 99
ChainResidueDetails
AGLU171metal ligand, proton acceptor, proton donor
AASN255metal ligand
AASP297metal ligand, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 99
ChainResidueDetails
CGLU171metal ligand, proton acceptor, proton donor
CASN255metal ligand
CASP297metal ligand, proton acceptor, proton donor

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PDB entries from 2024-07-17

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