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2YOB

High resolution AGXT_M structure

Functional Information from GO Data
ChainGOidnamespacecontents
A0004760molecular_functionserine-pyruvate transaminase activity
A0005515molecular_functionprotein binding
A0005777cellular_componentperoxisome
A0005782cellular_componentperoxisomal matrix
A0005829cellular_componentcytosol
A0006563biological_processL-serine metabolic process
A0007219biological_processNotch signaling pathway
A0008453molecular_functionalanine-glyoxylate transaminase activity
A0008483molecular_functiontransaminase activity
A0009436biological_processglyoxylate catabolic process
A0016597molecular_functionamino acid binding
A0019265biological_processglycine biosynthetic process, by transamination of glyoxylate
A0019448biological_processL-cysteine catabolic process
A0030170molecular_functionpyridoxal phosphate binding
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042853biological_processL-alanine catabolic process
A0043231cellular_componentintracellular membrane-bounded organelle
A0046487biological_processglyoxylate metabolic process
A0046724biological_processoxalic acid secretion
B0004760molecular_functionserine-pyruvate transaminase activity
B0005515molecular_functionprotein binding
B0005777cellular_componentperoxisome
B0005782cellular_componentperoxisomal matrix
B0005829cellular_componentcytosol
B0006563biological_processL-serine metabolic process
B0007219biological_processNotch signaling pathway
B0008453molecular_functionalanine-glyoxylate transaminase activity
B0008483molecular_functiontransaminase activity
B0009436biological_processglyoxylate catabolic process
B0016597molecular_functionamino acid binding
B0019265biological_processglycine biosynthetic process, by transamination of glyoxylate
B0019448biological_processL-cysteine catabolic process
B0030170molecular_functionpyridoxal phosphate binding
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042853biological_processL-alanine catabolic process
B0043231cellular_componentintracellular membrane-bounded organelle
B0046487biological_processglyoxylate metabolic process
B0046724biological_processoxalic acid secretion
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP A 1389
ChainResidue
ASER81
AGLN208
ALYS209
BTYR260
BTHR263
AGLY82
AHIS83
ATRP108
AGLY156
ASER158
AASP183
AVAL185
AALA186

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP B 1389
ChainResidue
ATYR260
ATHR263
BSER81
BGLY82
BHIS83
BTRP108
BGLY156
BSER158
BASP183
BVAL185
BALA186
BGLN208
BLYS209

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1390
ChainResidue
BARG258
BHOH2009
BHOH2073
BHOH2231
BHOH2303
BHOH2304

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BTB A 1390
ChainResidue
ATRP246
AASN249
AASP254
AMET259
AHOH2288
AHOH2290

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BTB B 1391
ChainResidue
AHOH2193
BLYS245
BTRP246
BASN249
BASP254
BGLN256
BMET259
BGOL1393
BHOH2221

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1391
ChainResidue
ALYS5
BARG197
BHIS342

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1392
ChainResidue
AASN72
ASER223
AASP224
AHOH2145
AHOH2260
AHOH2272

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1393
ChainResidue
ASER50
ALYS51
AHOH2109
AHOH2111
AHOH2389
AHOH2390
BGLN23
BMET340

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1394
ChainResidue
AMET38
AALA39
AGLY42
AHOH2092
AHOH2096
AHOH2392
BGLY42

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 1392
ChainResidue
BTHR135
BLEU136
BHOH2148
BHOH2307

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1395
ChainResidue
AVAL336
ASER337
AMET340
AHOH2347
AHOH2352
AHOH2356
AHOH2365
AHOH2393

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1393
ChainResidue
AHOH2182
AHOH2193
BLYS236
BTRP246
BBTB1391
BHOH2220

Functional Information from PROSITE/UniProt
site_idPS00595
Number of Residues21
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDILysGSQKalnappGtSlI
ChainResidueDetails
AILE200-ILE220

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AARG360
BARG360

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR9
BTHR9

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS209
BLYS209

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:O35423
ChainResidueDetails
ALYS225
BLYS225

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O35423
ChainResidueDetails
ALYS234
ALYS312
BLYS234
BLYS312

219140

PDB entries from 2024-05-01

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