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4N5N

Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase from Ralstonia eutropha in complexed with NADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0018454molecular_functionacetoacetyl-CoA reductase activity
A0042619biological_processpoly-hydroxybutyrate biosynthetic process
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0018454molecular_functionacetoacetyl-CoA reductase activity
B0042619biological_processpoly-hydroxybutyrate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues29
DetailsBINDING SITE FOR RESIDUE NAP A 301
ChainResidue
AGLY10
AGLY60
AASN61
AVAL62
AASN88
AALA89
ATHR111
AILE138
ASER139
ASER140
ATYR153
AMET12
ALYS157
APRO183
AGLY184
ATYR185
AILE186
ATHR188
AHOH425
AHOH443
AHOH452
AHOH513
AGLY13
AGLY14
AILE15
ACYS34
AGLY35
ASER38
AARG40

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAP B 301
ChainResidue
BGLY10
BGLY13
BGLY14
BILE15
BCYS34
BGLY35
BARG40
BGLY60
BASN61
BVAL62
BASN88
BALA89
BTHR111
BILE138
BSER139
BSER140
BTYR153
BLYS157
BPRO183
BGLY184
BILE186
BHOH459

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SvngqkgqfgQtnYSTAKAGLhGFTmALA
ChainResidueDetails
ASER140-ALA168

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR153
BTYR153

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:23913421
ChainResidueDetails
AGLY13
BGLY60
BASN88
BPRO183
AGLY35
AARG40
AGLY60
AASN88
APRO183
BGLY13
BGLY35
BARG40

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AASP94
AGLN147
AGLY184
AARG195
BASP94
BGLN147
BGLY184
BARG195

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PDB entries from 2024-08-21

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