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3K5P

Crystal structure of amino acid-binding ACT: D-isomer specific 2-hydroxyacid dehydrogenase catalytic domain from Brucella melitensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004617molecular_functionphosphoglycerate dehydrogenase activity
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 413
ChainResidue
AARG148
AASP206
ALYS231
ALYS232
AGLY233

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 414
ChainResidue
AASP182
ATHR183
AVAL212
APRO213

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 415
ChainResidue
APHE107
ASER108
ATHR110
AARG111
AARG151
AGLN166
AARG304

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 416
ChainResidue
AARG336
ATHR338
AGLY339
ATHR340
AARG341
AGLU384
ATYR412

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. LGIVGyGNIGsqvgnlaeslgmt.VRyYD
ChainResidueDetails
ALEU155-ASP182

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1psd
ChainResidueDetails
AHIS293
AGLU270

225946

PDB entries from 2024-10-09

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