2EH6
Crystal structure of acetylornithine aminotransferase from Aquifex aeolicus VF5
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 1001 |
| Chain | Residue |
| A | SER94 |
| A | LYS241 |
| A | HOH1007 |
| A | HOH1016 |
| A | HOH1103 |
| A | HOH1188 |
| B | THR270 |
| A | GLY95 |
| A | THR96 |
| A | PHE127 |
| A | HIS128 |
| A | GLU179 |
| A | ASP212 |
| A | VAL214 |
| A | GLN215 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP B 1002 |
| Chain | Residue |
| A | THR270 |
| A | HOH1008 |
| B | SER94 |
| B | GLY95 |
| B | THR96 |
| B | PHE127 |
| B | HIS128 |
| B | GLU179 |
| B | ASP212 |
| B | VAL214 |
| B | GLN215 |
| B | LYS241 |
| B | HOH1006 |
| B | HOH1015 |
| B | HOH1107 |
| B | HOH1110 |
| B | HOH1229 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIiDEVqt.GIgRtGefyayqhfnlkp....DVIalAKglgGG |
| Chain | Residue | Details |
| A | LEU209-GLY246 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of acetylornithine aminotransferase from Aquifex aeolicus vf5.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of acetylornithine aminotransferase from Aquifex aeolicus vf5.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of acetylornithine aminotransferase from Aquifex aeolicus vf5.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | LEU66 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | LEU66 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP212 | |
| A | LYS241 | |
| A | PHE127 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP212 | |
| B | LYS241 | |
| B | PHE127 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ASP212 | |
| A | PHE127 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| B | ASP212 | |
| B | PHE127 |
