2E54
Crystal structure of acetylornithine aminotransferase from Thermotoga maritima
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA A 1004 |
| Chain | Residue |
| A | LYS310 |
| A | TYR313 |
| A | VAL316 |
| A | NA1005 |
| A | HOH1043 |
| A | HOH1071 |
| A | HOH1073 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA A 1005 |
| Chain | Residue |
| A | HOH1071 |
| A | HOH1073 |
| A | HOH1203 |
| A | HOH1392 |
| A | HOH1474 |
| A | NA1004 |
| A | HOH1043 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP A 1001 |
| Chain | Residue |
| A | THR93 |
| A | GLY94 |
| A | THR95 |
| A | PHE126 |
| A | HIS127 |
| A | GLU178 |
| A | GLU183 |
| A | ASP211 |
| A | VAL213 |
| A | GLN214 |
| A | LYS240 |
| A | THR268 |
| A | HOH1024 |
| A | HOH1029 |
| A | HOH1030 |
| A | HOH1037 |
| A | HOH1040 |
| A | HOH1075 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1002 |
| Chain | Residue |
| A | GLU294 |
| A | LYS298 |
| A | LEU364 |
| A | THR365 |
| A | HOH1173 |
| A | HOH1336 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1003 |
| Chain | Residue |
| A | ASP32 |
| A | SER35 |
| A | ASN40 |
| A | HIS44 |
| A | PRO363 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LVfDEVqc.GMgRtGklfayqkygvvp....DVLttAKglgGG |
| Chain | Residue | Details |
| A | LEU208-GLY245 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| 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 Thermotoga maritima.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of acetylornithine aminotransferase (EC 2.6.1.11) (acoat) (tm1785) from Thermotoga maritima at 1.40 a resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| 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 Thermotoga maritima.","authoringGroup":["RIKEN structural genomics initiative (RSGI)"]}},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of acetylornithine aminotransferase (EC 2.6.1.11) (acoat) (tm1785) from Thermotoga maritima at 1.40 a resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| 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 (EC 2.6.1.11) (acoat) (tm1785) from Thermotoga maritima at 1.40 a resolution.","authoringGroup":["Joint center for structural genomics (JCSG)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | PHE126 | |
| A | ASP211 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | PHE126 | |
| A | ASP211 | |
| A | LYS240 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ay4 |
| Chain | Residue | Details |
| A | ARG48 |
