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5HXX

Crystal structure of AspAT from Corynebacterium glutamicum

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 PMP A 501
ChainResidue
ASER103
ASER256
ASER258
ALYS259
AAKG502
AHOH625
AHOH745
BTYR73
ASER104
ALEU105
ATYR142
AVAL186
AASN191
AASP220
AALA222
ATYR223

site_idAC2
Number of Residues9
Detailsbinding site for residue AKG A 502
ChainResidue
AGLY40
ATYR142
AARG144
ALYS259
APHE351
APMP501
AHOH726
AHOH817
BTYR73

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 503
ChainResidue
AARG13
APHE17
AASP20
AVAL345

site_idAC4
Number of Residues9
Detailsbinding site for residue GOL B 503
ChainResidue
BPHE189
BGLY194
BPHE195
BTHR196
BPRO346
BALA347
BHOH602
BHOH636
BHOH707

site_idAC5
Number of Residues8
Detailsbinding site for residue GOL B 504
ChainResidue
BALA336
BGLY339
BALA341
BTRP343
BHOH650
BHOH661
BHOH747
BHOH759

site_idAC6
Number of Residues23
Detailsbinding site for Di-peptide PLP B 501 and GLU B 502
ChainResidue
ATYR73
AILE289
BARG39
BGLY40
BLYS41
BSER103
BSER104
BLEU105
BTYR142
BARG144
BVAL186
BASN191
BASP220
BALA222
BTYR223
BSER256
BSER258
BLYS259
BARG394
BHOH601
BHOH625
BHOH682
BHOH779

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

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

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PDB entries from 2024-05-29

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