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

8GY2

Cryo-EM Structure of Membrane-Bound Alcohol Dehydrogenase from Gluconobacter oxydans

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0009055molecular_functionelectron transfer activity
A0016020cellular_componentmembrane
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0020037molecular_functionheme binding
A0030288cellular_componentouter membrane-bounded periplasmic space
B0005506molecular_functioniron ion binding
B0009055molecular_functionelectron transfer activity
B0016020cellular_componentmembrane
B0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
B0020037molecular_functionheme binding
Functional Information from PROSITE/UniProt
site_idPS00363
Number of Residues29
DetailsBACTERIAL_PQQ_1 Bacterial quinoprotein dehydrogenases signature 1. DWlsyGRsyseqrYSpldqINteNVgkLK
ChainResidueDetails
AASP53-LYS81

site_idPS00364
Number of Residues22
DetailsBACTERIAL_PQQ_2 Bacterial quinoprotein dehydrogenases signature 2. WdslvYDpvtDLVYLgvGngSP
ChainResidueDetails
ATRP279-PRO300

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues79
DetailsDomain: {"description":"Cytochrome c","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues31
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsCompositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q8GR64","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q8GR64","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"description":"covalent","evidences":[{"source":"UniProtKB","id":"Q8GR64","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"Q8GR64","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"PubMed","id":"9055427","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues103
DetailsDomain: {"description":"Cytochrome c 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues115
DetailsDomain: {"description":"Cytochrome c 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues90
DetailsDomain: {"description":"Cytochrome c 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues6
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues3
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon