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6F35

Crystal structure of the aspartate aminotranferase from Rhizobium meliloti

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
A0005737cellular_componentcytoplasm
A0006520biological_processamino acid metabolic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A0047536molecular_function2-aminoadipate transaminase activity
B0003824molecular_functioncatalytic activity
B0004069molecular_functionL-aspartate:2-oxoglutarate aminotransferase activity
B0005737cellular_componentcytoplasm
B0006520biological_processamino acid metabolic process
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
B0047536molecular_function2-aminoadipate transaminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue PLP A 501
ChainResidue
AGLY109
ALYS249
AARG257
AHOH639
BTYR74
BHOH714
AALA110
ALYS111
ATYR138
AASN181
AASP214
AMET216
ATYR217
ASER248

site_idAC2
Number of Residues7
Detailsbinding site for residue ACT A 502
ChainResidue
AGLY30
AGLY47
AALA378
AVAL380
AARG392
AHOH601
AHOH683

site_idAC3
Number of Residues5
Detailsbinding site for residue ACT A 503
ChainResidue
AGLY22
ATHR136
AASP140
AHOH613
AHOH619

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 504
ChainResidue
AASP52
APHE53
AARG311
AHOH761

site_idAC5
Number of Residues5
Detailsbinding site for residue ACT B 502
ChainResidue
BILE45
BGLY47
BVAL380
BARG392
BHOH629

site_idAC6
Number of Residues5
Detailsbinding site for residue ACT B 503
ChainResidue
APRO173
BHIS206
BPRO207
BHIS208
BHOH785

site_idAC7
Number of Residues5
Detailsbinding site for residue GOL B 504
ChainResidue
BASP52
BPHE53
BARG311
BTHR397
BHOH868

site_idAC8
Number of Residues22
Detailsbinding site for Di-peptide PLP B 501 and LYS B 249
ChainResidue
ATYR74
AHOH666
BGLY49
BPRO51
BGLY109
BALA110
BLYS111
BTRP135
BTYR138
BASN181
BASP214
BMET216
BTYR217
BVAL247
BSER248
BALA250
BTYR251
BALA252
BARG257
BHOH677
BHOH756
BHOH851

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GVSKayAMtGWRIG
ChainResidueDetails
AGLY246-GLY259

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00509
ChainResidueDetails
AGLY47
BGLY47

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q56232
ChainResidueDetails
ATRP135
AASN185
AARG392
BTRP135
BASN185
BARG392

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:30771275
ChainResidueDetails
ALYS249
BLYS249

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PDB entries from 2024-08-28

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