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3PPL

Crystal structure of an aspartate transaminase (NCgl0237, Cgl0240) from CORYNEBACTERIUM GLUTAMICUM ATCC 13032 KITASATO at 1.25 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
A0008483molecular_functiontransaminase activity
B0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
B0008483molecular_functiontransaminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP A 500
ChainResidue
ASER103
ASER256
ASER258
ALYS259
AHOH723
AHOH735
AHOH891
BTYR73
ASER104
ALEU105
ATYR142
AVAL186
AASN191
AASP220
AALA222
ATYR223

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP B 500
ChainResidue
ATYR73
BSER103
BSER104
BLEU105
BTYR142
BVAL186
BASN191
BASP220
BALA222
BTYR223
BSER256
BSER258
BLYS259
BHOH715
BHOH745
BHOH892

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 700
ChainResidue
BASP20
BALA321
BPHE324
BLEU328
BVAL345
BPRO346
BHOH776
BHOH1032
BHOH1862

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 701
ChainResidue
BGLN342
BTRP343
BHOH1316
BHOH1336

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|Ref.4
ChainResidueDetails
AARG39
ATYR142
AARG394
BARG39
BTYR142
BARG394

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:27355211, ECO:0000269|Ref.2, ECO:0000269|Ref.4
ChainResidueDetails
ASER103
AASN191
ATYR223
ASER256
BSER103
BASN191
BTYR223
BSER256

223790

PDB entries from 2024-08-14

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