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1X1T

Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase from Pseudomonas fragi Complexed with NAD+

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003858molecular_function3-hydroxybutyrate dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 301
ChainResidue
AASP38
AHIS128
AHOH501
AHOH502

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CAC A 302
ChainResidue
ANAD300
AHOH596
ASER142
AHIS144
ALYS152
ATYR155
ATRP257

site_idAC3
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAD A 300
ChainResidue
AGLY11
ATHR13
ASER14
AGLY15
AILE16
AGLY35
APHE36
AALA62
AASP63
ALEU64
AASN90
AALA91
AGLY92
ALEU113
AILE140
AALA141
ASER142
ATYR155
ALYS159
APRO185
AGLY186
ATRP187
AVAL188
ATHR190
ACAC302
AHOH519
AHOH667
AHOH673

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SahglvasanKsaYVAAKHGVvGFTkVTA
ChainResidueDetails
ASER142-ALA170

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ATYR155
ASER142
AASN114
ALYS159

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ALYS152
ALYS159

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ybv
ChainResidueDetails
ATYR155
ALYS159

221716

PDB entries from 2024-06-26

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