4H5U
Structural insights into yeast Nit2: wild-type yeast Nit2
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 | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 401 |
Chain | Residue |
A | ASP87 |
A | ASP116 |
A | LEU122 |
A | GOL403 |
A | HOH579 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 402 |
Chain | Residue |
A | HOH662 |
A | HOH710 |
B | ARG58 |
B | TYR59 |
A | ASP155 |
A | ILE156 |
A | HOH573 |
A | HOH604 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 403 |
Chain | Residue |
A | HIS117 |
A | PRO160 |
A | GOL401 |
A | HOH558 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 404 |
Chain | Residue |
A | ARG182 |
A | ARG292 |
A | ASN293 |
A | PRO296 |
A | HOH516 |
B | GLU98 |
B | LEU102 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 401 |
Chain | Residue |
A | ARG58 |
A | TYR59 |
A | HOH514 |
B | ASP155 |
B | ILE156 |
B | HOH519 |
B | HOH550 |
B | HOH569 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 402 |
Chain | Residue |
A | GLU98 |
B | ARG292 |
B | ASN293 |
B | PRO296 |
B | ASN299 |
B | GOL403 |
B | HOH508 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 403 |
Chain | Residue |
A | GLU98 |
A | HOH519 |
B | LYS163 |
B | GLY185 |
B | ALA186 |
B | ARG292 |
B | GOL402 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 404 |
Chain | Residue |
B | ARG209 |
B | TRP262 |
B | GLY263 |
B | LYS264 |
B | HOH577 |
B | HOH700 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CAC B 405 |
Chain | Residue |
A | HIS240 |
B | ILE68 |
B | GLU124 |
B | HOH553 |
B | HOH599 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL C 401 |
Chain | Residue |
B | ARG7 |
B | LEU280 |
B | HOH618 |
C | GLY226 |
C | MET227 |
C | HOH558 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 402 |
Chain | Residue |
A | ALA202 |
A | HIS203 |
C | ARG209 |
C | TRP262 |
C | GLY263 |
C | LYS264 |
C | HOH526 |
C | HOH698 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 401 |
Chain | Residue |
D | THR196 |
D | ILE197 |
D | LYS198 |
D | ARG249 |
D | ARG250 |
D | GLU251 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL D 402 |
Chain | Residue |
D | ARG209 |
D | TRP262 |
D | GLY263 |
D | LYS264 |
D | HOH550 |
D | HOH648 |
D | HOH649 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 403 |
Chain | Residue |
D | ARG182 |
D | GLN216 |
D | ARG292 |
D | PRO296 |
D | LEU297 |
D | TRP298 |
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 | CAF169 | |
B | CAF169 | |
C | CAF169 | |
D | CAF169 |
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 |