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1KQ3

CRYSTAL STRUCTURE OF A GLYCEROL DEHYDROGENASE (TM0423) FROM THERMOTOGA MARITIMA AT 1.5 A RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0006071biological_processglycerol metabolic process
A0008888molecular_functionglycerol dehydrogenase (NAD+) activity
A0016491molecular_functionoxidoreductase activity
A0016614molecular_functionoxidoreductase activity, acting on CH-OH group of donors
A0019588biological_processanaerobic glycerol catabolic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
AASP169
AHIS252
AHIS269
ATRS2922

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL A 501
ChainResidue
ATRS2922
AHOH2932
AASP119
AASP169
ATHR173
ASER239
AHIS252

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRS A 2922
ChainResidue
AASP119
AASP169
APHE243
AHIS252
AHIS269
AZN401
ACL501
AHOH3121

Functional Information from PROSITE/UniProt
site_idPS00060
Number of Residues21
DetailsADH_IRON_2 Iron-containing alcohol dehydrogenases signature 2. SgLGfeSGgLAAahaIhNGlT
ChainResidueDetails
ASER239-THR259

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. FESGGLAA
ChainResidueDetails
APHE243-ALA250

site_idPS00913
Number of Residues29
DetailsADH_IRON_1 Iron-containing alcohol dehydrogenases signature 1. VLvDteivakaParflVaGmgDALatwfE
ChainResidueDetails
AVAL148-GLU176

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P32816
ChainResidueDetails
AASP37
AGLY92
ALYS93
ATHR114
ASER117
ASER123
ALEU125
ATYR129

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:12193646, ECO:0007744|PDB:1KQ3
ChainResidueDetails
AASP119

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:12193646, ECO:0007744|PDB:1KQ3
ChainResidueDetails
AASP169
AHIS252
AHIS269

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqs
ChainResidueDetails
AASN256

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dqs
ChainResidueDetails
AHIS252

site_idMCSA1
Number of Residues4
DetailsM-CSA 312
ChainResidueDetails
AASP169metal ligand
AHIS252metal ligand
AHIS255hydrogen bond acceptor, increase basicity
AHIS269metal ligand

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PDB entries from 2024-07-24

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