4HG5
Structural insights into yeast Nit2: wild-type yeast Nit2 in complex with oxaloacetate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005575 | cellular_component | cellular_component |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| A | 0043605 | biological_process | amide catabolic process |
| A | 0050406 | molecular_function | [acetyl-CoA carboxylase]-phosphatase activity |
| A | 0110050 | molecular_function | deaminated glutathione amidase activity |
| B | 0005575 | cellular_component | cellular_component |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| B | 0043605 | biological_process | amide catabolic process |
| B | 0050406 | molecular_function | [acetyl-CoA carboxylase]-phosphatase activity |
| B | 0110050 | molecular_function | deaminated glutathione amidase activity |
| C | 0005575 | cellular_component | cellular_component |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| C | 0043605 | biological_process | amide catabolic process |
| C | 0050406 | molecular_function | [acetyl-CoA carboxylase]-phosphatase activity |
| C | 0110050 | molecular_function | deaminated glutathione amidase activity |
| D | 0005575 | cellular_component | cellular_component |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| D | 0043605 | biological_process | amide catabolic process |
| D | 0050406 | molecular_function | [acetyl-CoA carboxylase]-phosphatase activity |
| D | 0110050 | molecular_function | deaminated glutathione amidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OAA A 401 |
| Chain | Residue |
| A | LYS127 |
| A | PHE131 |
| A | CYS169 |
| A | TYR170 |
| A | ARG173 |
| A | PHE195 |
| A | THR196 |
| A | THR199 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 402 |
| Chain | Residue |
| A | ILE156 |
| A | HOH580 |
| A | HOH612 |
| B | ARG58 |
| B | TYR59 |
| B | HOH572 |
| A | ASP155 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 403 |
| Chain | Residue |
| A | ASP87 |
| A | ASP116 |
| A | PRO160 |
| A | HOH531 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CAC A 404 |
| Chain | Residue |
| A | HIS240 |
| B | ILE68 |
| B | LEU94 |
| B | GLU124 |
| B | HOH597 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CAC A 405 |
| Chain | Residue |
| A | LEU94 |
| A | ILE121 |
| A | GLU124 |
| A | HOH537 |
| B | HIS240 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OAA B 401 |
| Chain | Residue |
| B | LYS127 |
| B | PHE131 |
| B | CYS169 |
| B | TYR170 |
| B | ARG173 |
| B | PHE195 |
| B | THR196 |
| B | THR199 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 402 |
| Chain | Residue |
| B | LYS36 |
| B | LEU278 |
| B | ILE279 |
| B | LEU280 |
| C | ARG249 |
| C | GLU251 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 403 |
| Chain | Residue |
| B | ARG7 |
| C | CYS14 |
| C | GLY226 |
| C | MET227 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 404 |
| Chain | Residue |
| A | GLU98 |
| A | HOH539 |
| B | LYS163 |
| B | GLY185 |
| B | ALA186 |
| B | ARG292 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 405 |
| Chain | Residue |
| A | ARG58 |
| A | TYR59 |
| A | HOH529 |
| B | ASP155 |
| B | ILE156 |
| B | HOH564 |
| B | HOH568 |
| B | HOH588 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OAA C 401 |
| Chain | Residue |
| C | PHE131 |
| C | CYS169 |
| C | TYR170 |
| C | ARG173 |
| C | ALA194 |
| C | PHE195 |
| C | THR199 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 402 |
| Chain | Residue |
| A | GLN300 |
| C | LEU128 |
| C | LEU130 |
| C | HOH583 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 403 |
| Chain | Residue |
| C | GLN123 |
| C | GLU124 |
| C | ILE153 |
| C | PRO154 |
| C | ASP155 |
| C | HOH532 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OAA D 401 |
| Chain | Residue |
| D | LYS127 |
| D | PHE131 |
| D | CYS169 |
| D | TYR170 |
| D | ARG173 |
| D | PHE195 |
| D | THR196 |
| D | THR199 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 402 |
| Chain | Residue |
| B | ARG209 |
| B | TRP262 |
| B | GLY263 |
| B | LYS264 |
| D | ALA202 |
| D | HIS203 |
| D | HOH556 |
Functional Information from PROSITE/UniProt
| site_id | PS01227 |
| Number of Residues | 21 |
| Details | UPF0012 Uncharacterized protein family UPF0012 signature. GsaICYDIrFPefslklrsmG |
| Chain | Residue | Details |
| A | GLY165-GLY185 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 279 |
| Details | Domain: {"description":"CN hydrolase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00054","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00054","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00054","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU00054","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23897470","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23897470","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
