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5OG0

Crystal structure of human Alanine:Glyoxylate Aminotransferase major allele (AGT-Ma) at 2.5 Angstrom; internal aldimine with PLP in the active site

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
A0016740molecular_functiontransferase activity
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
A0043621molecular_functionobsolete protein self-association
A0046487biological_processglyoxylate metabolic process
A0046724biological_processoxalic acid secretion
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue PLP A 401
ChainResidue
ASER81
AGLN208
ALYS209
ATYR260
ATHR263
AGLY82
AHIS83
ATRP108
AGLY156
ASER158
AASP183
AVAL185
AALA186

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 Residues1
DetailsBINDING:
ChainResidueDetails
AARG360

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATHR9

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS209

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:O35423
ChainResidueDetails
ALYS225

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O35423
ChainResidueDetails
ALYS234
ALYS312

218853

PDB entries from 2024-04-24

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