5IE0
Crystal structure of a plant enzyme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006952 | biological_process | defense response |
| A | 0009506 | cellular_component | plasmodesma |
| A | 0009507 | cellular_component | chloroplast |
| A | 0009570 | cellular_component | chloroplast stroma |
| A | 0010030 | biological_process | positive regulation of seed germination |
| A | 0010214 | biological_process | seed coat development |
| A | 0016874 | molecular_function | ligase activity |
| A | 0031956 | molecular_function | medium-chain fatty acid-CoA ligase activity |
| A | 0033611 | biological_process | oxalate catabolic process |
| A | 0048046 | cellular_component | apoplast |
| A | 0050203 | molecular_function | oxalate-CoA ligase activity |
| A | 0050832 | biological_process | defense response to fungus |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006952 | biological_process | defense response |
| B | 0009506 | cellular_component | plasmodesma |
| B | 0009507 | cellular_component | chloroplast |
| B | 0009570 | cellular_component | chloroplast stroma |
| B | 0010030 | biological_process | positive regulation of seed germination |
| B | 0010214 | biological_process | seed coat development |
| B | 0016874 | molecular_function | ligase activity |
| B | 0031956 | molecular_function | medium-chain fatty acid-CoA ligase activity |
| B | 0033611 | biological_process | oxalate catabolic process |
| B | 0048046 | cellular_component | apoplast |
| B | 0050203 | molecular_function | oxalate-CoA ligase activity |
| B | 0050832 | biological_process | defense response to fungus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue SRT A 1001 |
| Chain | Residue |
| A | HIS214 |
| A | HOH1146 |
| A | HOH1164 |
| A | HOH1383 |
| A | HOH1387 |
| A | VAL215 |
| A | HIS216 |
| A | SER289 |
| A | ALA313 |
| A | MET314 |
| A | THR315 |
| A | HIS319 |
| A | LYS500 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue SRT A 1002 |
| Chain | Residue |
| A | ARG20 |
| A | ARG21 |
| A | SER205 |
| A | ASN253 |
| A | HOH1121 |
| A | HOH1178 |
| A | HOH1272 |
| A | HOH1372 |
| A | HOH1403 |
| B | ASP162 |
| B | HOH797 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue SRT B 601 |
| Chain | Residue |
| B | HIS214 |
| B | VAL215 |
| B | HIS216 |
| B | SER289 |
| B | ALA313 |
| B | MET314 |
| B | THR315 |
| B | HIS319 |
| B | LYS500 |
| B | HOH720 |
| B | HOH802 |
| B | HOH893 |
| B | HOH980 |
| B | HOH990 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue SRT B 602 |
| Chain | Residue |
| A | ASP162 |
| A | HOH1607 |
| B | ARG20 |
| B | ARG21 |
| B | SER205 |
| B | ASN253 |
| B | HOH701 |
| B | HOH707 |
| B | HOH717 |
| B | HOH778 |
| B | HOH842 |
| B | HOH880 |
| B | HOH975 |
Functional Information from PROSITE/UniProt
| site_id | PS00455 |
| Number of Residues | 12 |
| Details | AMP_BINDING Putative AMP-binding domain signature. FLHTSGTTSrPK |
| Chain | Residue | Details |
| A | PHE167-LYS178 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 138 |
| Details | Region: {"description":"SBD1","evidences":[{"source":"UniProtKB","id":"Q42524","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 126 |
| Details | Region: {"description":"SBD2","evidences":[{"source":"UniProtKB","id":"Q42524","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27326693","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IE2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IE3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27326693","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IE2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O24146","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27326693","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IE3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
