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3ISL

Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucG) from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000256biological_processallantoin catabolic process
A0003824molecular_functioncatalytic activity
A0004760molecular_functionserine-pyruvate transaminase activity
A0005777cellular_componentperoxisome
A0006144biological_processpurine nucleobase metabolic process
A0008453molecular_functionalanine-glyoxylate transaminase activity
A0008483molecular_functiontransaminase activity
A0019265biological_processglycine biosynthetic process, by transamination of glyoxylate
B0000256biological_processallantoin catabolic process
B0003824molecular_functioncatalytic activity
B0004760molecular_functionserine-pyruvate transaminase activity
B0005777cellular_componentperoxisome
B0006144biological_processpurine nucleobase metabolic process
B0008453molecular_functionalanine-glyoxylate transaminase activity
B0008483molecular_functiontransaminase activity
B0019265biological_processglycine biosynthetic process, by transamination of glyoxylate
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PLP A 419
ChainResidue
ATHR72
BHIS268
BTHR269
ASER73
AARG74
APHE99
AGLY147
ATHR149
AASP174
AGLN199
ALYS200

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PLP B 419
ChainResidue
ATHR269
BTHR72
BSER73
BARG74
BPHE99
BGLY147
BTHR149
BASP174
BGLN199
BLYS200

Functional Information from PROSITE/UniProt
site_idPS00595
Number of Residues21
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDAAigGTQKclsvpsGmApI
ChainResidueDetails
AILE191-ILE211

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:20852637
ChainResidueDetails
ALYS200
BLYS200

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PDB entries from 2024-07-17

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