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3VZP

Crystal structure of PhaB from Ralstonia eutropha

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
C0005737cellular_componentcytoplasm
C0016491molecular_functionoxidoreductase activity
C0018454molecular_functionacetoacetyl-CoA reductase activity
C0042619biological_processpoly-hydroxybutyrate biosynthetic process
D0005737cellular_componentcytoplasm
D0016491molecular_functionoxidoreductase activity
D0018454molecular_functionacetoacetyl-CoA reductase activity
D0042619biological_processpoly-hydroxybutyrate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AGLY13
AGLY14
ATHR188
AASP189
AMET190
AHOH421

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AARG40
ACYS34
AGLY35
ASER38

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AARG210
AHOH444
AHOH531
AHOH582
CGLY175

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 304
ChainResidue
ATHR101
AARG102
BASN37
BHOH532
DTRP65

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DIO A 305
ChainResidue
AASN142
AGLN150
ATYR185
AHOH507

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 301
ChainResidue
BGLY14
BTHR188
BASP189
BMET190
BHOH409

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BCYS34
BGLY35
BSER38
BARG40

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 303
ChainResidue
AASN61
AALA63
AASP64
AASP110
BASP64
BHOH542

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DIO B 304
ChainResidue
BASN142
BGLN150
BMET190
BHOH421

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DIO B 305
ChainResidue
BGLN3
BARG4
BGLY27

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 301
ChainResidue
CGLY13
CGLY14
CTHR188
CASP189
CMET190
CHOH548

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DIO C 302
ChainResidue
CASN142
CGLN150
CTYR185
CHOH445
CHOH467

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DIO C 303
ChainResidue
CARG4
CGLY27
CPHE28

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 301
ChainResidue
DGLY13
DGLY14
DTHR188
DASP189
DMET190

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DIO D 302
ChainResidue
DGLN3
DARG4
DGLY27
DHOH529

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DIO D 303
ChainResidue
DASN142
DGLN150
DHOH420
DHOH454

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 Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10001
ChainResidueDetails
ATYR153
BTYR153
CTYR153
DTYR153

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:23913421
ChainResidueDetails
AASN88
APRO183
BGLY13
BGLY35
BARG40
BGLY60
BASN88
BPRO183
CGLY13
CGLY35
CARG40
CGLY60
CASN88
CPRO183
DGLY13
DGLY35
DARG40
DGLY60
DASN88
DPRO183
AGLY13
AGLY35
AARG40
AGLY60

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING:
ChainResidueDetails
BASP94
BGLN147
BGLY184
BARG195
CASP94
CGLN147
CGLY184
CARG195
DASP94
DGLN147
DGLY184
DARG195
AGLN147
AGLY184
AARG195
AASP94

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PDB entries from 2024-06-12

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