4HG3
Structural insights into yeast Nit2: wild-type yeast Nit2 in complex with alpha-ketoglutarate
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 | 9 |
| Details | BINDING SITE FOR RESIDUE AKG A 401 |
| Chain | Residue |
| A | LYS127 |
| A | PHE131 |
| A | CYS169 |
| A | TYR170 |
| A | ARG173 |
| A | PHE195 |
| A | THR196 |
| A | THR199 |
| A | HOH543 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 402 |
| Chain | Residue |
| A | ARG58 |
| A | TYR59 |
| A | HOH525 |
| A | HOH532 |
| A | HOH641 |
| B | ASP155 |
| B | ILE156 |
| B | HOH531 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 403 |
| Chain | Residue |
| A | HIS117 |
| A | PRO160 |
| A | HOH542 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 404 |
| Chain | Residue |
| A | ASP155 |
| A | ILE156 |
| A | HOH502 |
| A | HOH561 |
| A | HOH584 |
| A | HOH627 |
| B | ARG58 |
| B | TYR59 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 405 |
| Chain | Residue |
| A | ARG292 |
| A | ASN293 |
| A | PRO296 |
| A | ASN299 |
| A | HOH523 |
| B | GLU98 |
| B | LEU102 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 406 |
| Chain | Residue |
| A | HOH639 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 407 |
| Chain | Residue |
| A | ARG209 |
| A | TRP262 |
| A | GLY263 |
| A | LYS264 |
| A | HOH596 |
| A | HOH631 |
| C | ALA202 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 408 |
| Chain | Residue |
| A | TYR59 |
| A | LYS63 |
| A | ASP232 |
| A | GLU234 |
| B | LYS151 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CAC A 409 |
| Chain | Residue |
| A | ILE68 |
| A | GLU124 |
| A | HOH626 |
| B | HIS240 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CAC A 410 |
| Chain | Residue |
| A | GLU45 |
| A | HIS93 |
| A | GLU143 |
| A | ARG250 |
| A | HOH519 |
| A | HOH597 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AKG B 401 |
| Chain | Residue |
| B | LYS127 |
| B | PHE131 |
| B | CYS169 |
| B | TYR170 |
| B | ARG173 |
| B | ALA194 |
| B | PHE195 |
| B | THR196 |
| B | THR199 |
| B | HOH578 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 402 |
| Chain | Residue |
| A | GLU98 |
| B | ARG292 |
| B | ASN293 |
| B | PRO296 |
| B | ASN299 |
| B | HOH508 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 403 |
| Chain | Residue |
| B | LYS36 |
| B | LEU278 |
| B | HOH567 |
| C | GLU251 |
| C | GOL403 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 404 |
| Chain | Residue |
| A | GLU98 |
| A | LEU101 |
| B | LYS163 |
| B | GLY185 |
| B | ALA186 |
| B | ARG292 |
| B | HOH583 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 405 |
| Chain | Residue |
| B | ARG209 |
| B | TRP262 |
| B | GLY263 |
| B | LYS264 |
| B | HOH522 |
| B | HOH584 |
| B | HOH604 |
| D | ALA202 |
| D | HIS203 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 406 |
| Chain | Residue |
| C | LEU305 |
| A | LYS151 |
| B | TYR59 |
| B | LYS63 |
| B | ASP232 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CAC B 407 |
| Chain | Residue |
| A | HIS240 |
| B | LEU94 |
| B | GLU124 |
| B | HOH616 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CAC B 408 |
| Chain | Residue |
| B | GLU45 |
| B | LEU50 |
| B | HIS93 |
| B | GLU143 |
| B | ARG250 |
| B | HOH524 |
| B | HOH589 |
| site_id | CC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AKG C 401 |
| Chain | Residue |
| C | LYS127 |
| C | PHE131 |
| C | CYS169 |
| C | TYR170 |
| C | ARG173 |
| C | ALA194 |
| C | PHE195 |
| C | THR196 |
| C | THR199 |
| C | HOH619 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 402 |
| Chain | Residue |
| C | SER73 |
| C | THR76 |
| C | HOH538 |
| C | HOH620 |
| site_id | CC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 403 |
| Chain | Residue |
| B | ARG7 |
| B | LEU280 |
| B | GOL403 |
| C | CYS14 |
| C | GLY226 |
| C | MET227 |
| C | HOH563 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CAC C 404 |
| Chain | Residue |
| C | SER51 |
| C | ASN53 |
| C | SER146 |
| C | ARG250 |
| C | CAC405 |
| site_id | CC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CAC C 405 |
| Chain | Residue |
| C | GLU45 |
| C | LEU50 |
| C | HIS93 |
| C | ASN110 |
| C | GLU143 |
| C | VAL147 |
| C | ARG250 |
| C | CAC404 |
| C | HOH657 |
| site_id | CC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE AKG D 401 |
| Chain | Residue |
| D | LYS127 |
| D | PHE131 |
| D | CYS169 |
| D | TYR170 |
| D | ARG173 |
| D | ALA194 |
| D | PHE195 |
| D | THR196 |
| D | THR199 |
| site_id | CC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 402 |
| Chain | Residue |
| B | ALA202 |
| B | HIS203 |
| D | ARG209 |
| D | TRP262 |
| D | GLY263 |
| D | HOH548 |
| D | HOH578 |
| site_id | CC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 403 |
| Chain | Residue |
| D | THR196 |
| D | ILE197 |
| D | LYS198 |
| D | ARG249 |
| D | ARG250 |
| D | GLU251 |
| D | HOH596 |
| site_id | CC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CAC D 404 |
| Chain | Residue |
| D | GLU45 |
| D | HIS93 |
| D | GLU143 |
| D | VAL147 |
| D | ARG250 |
| D | HOH576 |
| D | HOH598 |
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 | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00054 |
| Chain | Residue | Details |
| A | GLU45 | |
| B | GLU45 | |
| C | GLU45 | |
| D | GLU45 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU00054 |
| Chain | Residue | Details |
| A | LYS127 | |
| B | LYS127 | |
| C | LYS127 | |
| D | LYS127 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00054, ECO:0000269|PubMed:23897470 |
| Chain | Residue | Details |
| A | CYS169 | |
| B | CYS169 | |
| C | CYS169 | |
| D | CYS169 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23897470 |
| Chain | Residue | Details |
| A | ARG173 | |
| A | THR199 | |
| B | ARG173 | |
| B | THR199 | |
| C | ARG173 | |
| C | THR199 | |
| D | ARG173 | |
| D | THR199 |
