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

1W6S

The high resolution structure of methanol dehydrogenase from methylobacterium extorquens

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 A1599
ChainResidue
AGLU177
AASN261
AASP303
APQQ1596

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C3599
ChainResidue
CGLU2177
CASN2261
CASP2303
CPQQ3597

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE PQQ A1596
ChainResidue
ACYS104
AVAL107
AARG109
ATHR159
ASER174
AGLY175
AALA176
AGLU177
ATHR241
ATRP243
AASN261
AARG331
AASN394
ATRP476
AGLY539
ATRP540
ACA1599
AHOH2329
AHOH2602
AGLU55

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE PQQ C3597
ChainResidue
CGLU2055
CCYS2104
CVAL2107
CARG2109
CTHR2159
CSER2174
CGLY2175
CALA2176
CGLU2177
CTHR2241
CTRP2243
CASN2261
CARG2331
CASN2394
CTRP2476
CGLY2539
CTRP2540
CCA3599
CHOH4356
CHOH4609

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A1597
ChainResidue
AALA43
AGLY584
APRO585
ATYR586
AASP587
AHOH2603
AHOH2604
CARG2041
CTRP2508
CLYS2509

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A1598
ChainResidue
AHIS525
ATHR528
ATYR530
ALYS583
APRO585
AHOH2132
AHOH2135
AHOH2605

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL C3598
ChainResidue
ATRP508
ALYS509
AHOH2095
CALA2043
CGLY2582
CGLY2584
CPRO2585
CTYR2586
CASP2587
CHOH4610

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
CASP2303

249697

PDB entries from 2026-02-25

PDB statisticsPDBj update infoContact PDBjnumon