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4PN3

Crystal structure of 3-hydroxyacyl-CoA-dehydrogenase from Brucella melitensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
B0016491molecular_functionoxidoreductase activity
C0016491molecular_functionoxidoreductase activity
D0016491molecular_functionoxidoreductase activity
E0016491molecular_functionoxidoreductase activity
F0016491molecular_functionoxidoreductase activity
G0016491molecular_functionoxidoreductase activity
H0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue TRS B 301
ChainResidue
AGLU242
AVAL243
AARG245
BPHE152
BGLU242
BVAL243

site_idAC2
Number of Residues7
Detailsbinding site for residue TRS D 301
ChainResidue
CARG245
DPHE152
DGLU242
DVAL243
CPHE152
CGLU242
CVAL243

site_idAC3
Number of Residues10
Detailsbinding site for residue TRS F 301
ChainResidue
EPHE152
EGLU242
EVAL243
EARG245
FGLU242
FVAL243
FHOH430
FHOH439
FHOH456
FHOH463

site_idAC4
Number of Residues7
Detailsbinding site for residue TRS G 301
ChainResidue
GGLU242
GVAL243
GARG245
GHOH430
HGLU242
HVAL243
HARG245

Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. SvaafdgqigQaaYSASKGGVaAMTlPVA
ChainResidueDetails
ASER148-ALA176

227344

PDB entries from 2024-11-13

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