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4N5M

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

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 Residues19
DetailsBINDING SITE FOR RESIDUE CAA A 301
ChainResidue
AASP94
AMET190
AVAL191
AARG195
AHOH497
AHOH506
AHOH543
AHOH548
AHOH582
AHOH598
AHOH612
AGLN147
APHE148
AGLY149
AGLN150
ATYR153
AGLY184
ATYR185
AILE186

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
AASN37
ATHR101
AARG102
AGOL303
BTRP65

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
AARG98
ALYS99
AMET100
AGOL302
AHOH536
AHOH630
BLYS121

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
AGLY60
AASN61
AVAL62
ATHR111
AHOH434
AHOH539
AHOH643
AHOH653

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE CAA B 301
ChainResidue
BASP94
BASN142
BGLN147
BPHE148
BGLY149
BGLN150
BTYR153
BGLY184
BTYR185
BVAL191
BARG195
BILE202
BHOH506
BHOH517
BHOH522
BHOH534
BHOH594
BHOH638

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 302
ChainResidue
BGLN3
BARG4
BASP26
BGLY27
BPHE28
BHOH446
BHOH508
BHOH564
BHOH568

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 303
ChainResidue
BTYR7
BTHR9
BGLY10
BGLY33
BCYS34
BSER58
BGLY60
BHOH402
BHOH654

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 304
ChainResidue
BGLY35
BASN61
BHOH654

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
AARG40
AGLY60
AASN88
APRO183
BGLY13
BGLY35
BARG40
BGLY60
BASN88
BPRO183
AGLY13
AGLY35

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

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PDB entries from 2024-05-15

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