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3F6T

Crystal structure of aspartate aminotransferase (E.C. 2.6.1.1) (YP_194538.1) from Lactobacillus acidophilus NCFM at 2.15 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
A0006520biological_processamino acid metabolic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
A0030170molecular_functionpyridoxal phosphate binding
B0003824molecular_functioncatalytic activity
B0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
B0006520biological_processamino acid metabolic process
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0016740molecular_functiontransferase activity
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 533
ChainResidue
AILE68
AASN70
AMSE73
AHOH704
AHOH788
BASN69
BILE413
BHOH586

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 534
ChainResidue
AARG116
ALYS194
ASER243
AHOH602
AHOH790
AARG83

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 535
ChainResidue
ATYR76
AASN130
AHOH581
AHOH582
AHOH584

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 536
ChainResidue
AHIS181
AARG350
AASP370
ASER373
AHOH562
BPRO209
BGLU210
BHOH694

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 533
ChainResidue
AASN41
APRO42
BTYR76
BASN130
BHOH538
BHOH539
BHOH712

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP283
APHE202

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BASP283
BPHE202

237735

PDB entries from 2025-06-18

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