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4A2C

Crystal structure of galactitol-1-phosphate dehydrogenase from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0008868molecular_functiongalactitol-1-phosphate 5-dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019402biological_processgalactitol metabolic process
A0019404biological_processgalactitol catabolic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0008868molecular_functiongalactitol-1-phosphate 5-dehydrogenase activity
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019402biological_processgalactitol metabolic process
B0019404biological_processgalactitol catabolic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI A 1347
ChainResidue
ACYS38
AHIS59
AGLU60
AGLU144

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI A 1348
ChainResidue
AHIS267
AGLU300
AHOH2238
BHIS267

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1349
ChainResidue
APHE90
ACYS92
ACYS95
ACYS103
ACYS89

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI B 1347
ChainResidue
BCYS38
BHIS59
BGLU60
BGLU144
BHOH2165

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1348
ChainResidue
BCYS89
BCYS92
BCYS95
BCYS103

Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEfSGYidavGsgV
ChainResidueDetails
AGLY58-VAL72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ACYS38
BCYS89
BCYS92
BCYS95
BCYS103
BGLU144
AHIS59
ACYS89
ACYS92
ACYS95
ACYS103
AGLU144
BCYS38
BHIS59

237735

PDB entries from 2025-06-18

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