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6ZZS

Crystal structure of (R)-3-hydroxybutyrate dehydrogenase from Acinetobacter baumannii complexed with NAD+ and 3-oxovalerate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003858molecular_function3-hydroxybutyrate dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
B0000166molecular_functionnucleotide binding
B0003858molecular_function3-hydroxybutyrate dehydrogenase activity
B0016491molecular_functionoxidoreductase activity
C0000166molecular_functionnucleotide binding
C0003858molecular_function3-hydroxybutyrate dehydrogenase activity
C0016491molecular_functionoxidoreductase activity
D0000166molecular_functionnucleotide binding
D0003858molecular_function3-hydroxybutyrate dehydrogenase activity
D0016491molecular_functionoxidoreductase activity
E0000166molecular_functionnucleotide binding
E0003858molecular_function3-hydroxybutyrate dehydrogenase activity
E0016491molecular_functionoxidoreductase activity
F0000166molecular_functionnucleotide binding
F0003858molecular_function3-hydroxybutyrate dehydrogenase activity
F0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues27
Detailsbinding site for residue NAD A 301
ChainResidue
AGLY14
AASN91
AALA92
AGLY93
AVAL114
AALA142
ATYR156
ALYS160
APRO186
AGLY187
AVAL189
ASER17
ATHR191
ALEU193
AVAL194
AQT8302
AHOH410
AHOH411
AHOH424
AHOH460
AGLY18
AILE19
AASP38
AMET39
ACYS63
AASP64
AVAL65

site_idAC2
Number of Residues7
Detailsbinding site for residue QT8 A 302
ChainResidue
AGLN95
ASER143
AASN145
ATYR156
ALEU193
AGLN197
ANAD301

site_idAC3
Number of Residues28
Detailsbinding site for residue NAD B 301
ChainResidue
BGLY14
BSER17
BGLY18
BILE19
BASP38
BMET39
BCYS63
BASP64
BVAL65
BASN91
BALA92
BGLY93
BVAL114
BMET141
BALA142
BSER143
BTYR156
BLYS160
BPRO186
BGLY187
BVAL189
BTHR191
BVAL194
BQT8302
BHOH404
BHOH430
BHOH444
BHOH459

site_idAC4
Number of Residues7
Detailsbinding site for residue QT8 B 302
ChainResidue
BGLN95
BSER143
BASN145
BLYS153
BGLN197
BNAD301
BHOH418

site_idAC5
Number of Residues29
Detailsbinding site for residue NAD C 301
ChainResidue
CGLY14
CSER17
CGLY18
CILE19
CASP38
CMET39
CCYS63
CASP64
CVAL65
CASN91
CALA92
CGLY93
CVAL114
CMET141
CALA142
CSER143
CTYR156
CLYS160
CPRO186
CGLY187
CVAL189
CTHR191
CLEU193
CVAL194
CQT8302
CQT8303
CHOH401
CHOH402
CHOH456

site_idAC6
Number of Residues9
Detailsbinding site for residue QT8 C 302
ChainResidue
CSER143
CASN145
CLYS153
CTYR156
CLEU193
CGLN197
CNAD301
CHOH473
CGLN95

site_idAC7
Number of Residues5
Detailsbinding site for residue QT8 C 303
ChainResidue
CMET39
CASP64
CPHE94
CLYS110
CNAD301

site_idAC8
Number of Residues28
Detailsbinding site for residue NAD D 301
ChainResidue
DGLY14
DSER17
DGLY18
DILE19
DASP38
DMET39
DCYS63
DASP64
DVAL65
DASN91
DALA92
DGLY93
DVAL114
DMET141
DALA142
DSER143
DTYR156
DLYS160
DPRO186
DGLY187
DVAL189
DTHR191
DLEU193
DVAL194
DQT8302
DHOH402
DHOH403
DHOH468

site_idAC9
Number of Residues8
Detailsbinding site for residue QT8 D 302
ChainResidue
DGLN95
DSER143
DASN145
DLYS153
DTYR156
DLEU193
DGLN197
DNAD301

site_idAD1
Number of Residues27
Detailsbinding site for residue NAD E 301
ChainResidue
EGLY14
ESER17
EGLY18
EILE19
EASP38
EMET39
ECYS63
EASP64
EVAL65
EASN91
EALA92
EGLY93
EVAL114
EMET141
EALA142
ESER143
ETYR156
ELYS160
EGLY187
ETYR188
EVAL189
ETHR191
ELEU193
EVAL194
EHOH402
EHOH408
EHOH440

site_idAD2
Number of Residues24
Detailsbinding site for residue NAD F 301
ChainResidue
FGLY14
FSER17
FGLY18
FILE19
FASP38
FMET39
FCYS63
FASP64
FVAL65
FASN91
FGLY93
FVAL114
FMET141
FALA142
FSER143
FTYR156
FLYS160
FPRO186
FGLY187
FVAL189
FTHR191
FVAL194
FQT8302
FHOH405

site_idAD3
Number of Residues7
Detailsbinding site for residue QT8 F 302
ChainResidue
FGLN95
FSER143
FASN145
FLYS153
FTYR156
FGLN197
FNAD301

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SingligfagKagYNSAKHGViGLTkVAA
ChainResidueDetails
ASER143-ALA171

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PDB entries from 2024-07-24

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