4HGD
Structural insights into yeast Nit2: C169S mutant of yeast Nit2 in complex with an endogenous peptide-like ligand
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 GOL A 401 |
Chain | Residue |
A | ARG58 |
A | TYR59 |
A | HOH510 |
A | HOH571 |
A | HOH591 |
B | ASP155 |
B | ILE156 |
B | HOH599 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 402 |
Chain | Residue |
A | ILE156 |
A | HOH558 |
A | HOH577 |
A | HOH592 |
B | ARG58 |
B | TYR59 |
B | HOH511 |
A | ASP155 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 403 |
Chain | Residue |
A | LYS36 |
A | LEU278 |
A | ILE279 |
A | LEU280 |
C | ARG249 |
C | GLU251 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 404 |
Chain | Residue |
A | GLY185 |
A | ALA186 |
A | ARG292 |
B | GLU98 |
B | LEU101 |
B | HOH516 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 405 |
Chain | Residue |
A | PRO139 |
A | THR196 |
A | ILE197 |
A | LYS198 |
A | GLU251 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CAC A 406 |
Chain | Residue |
A | ILE68 |
A | ILE121 |
A | GLU124 |
B | HIS240 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE KGT A 407 |
Chain | Residue |
A | GLU45 |
A | HIS93 |
A | LYS127 |
A | PHE131 |
A | GLU143 |
A | SER169 |
A | TYR170 |
A | ARG173 |
A | ALA194 |
A | PHE195 |
A | THR196 |
A | THR199 |
A | ARG250 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 401 |
Chain | Residue |
A | LYS151 |
B | TYR59 |
B | LYS63 |
B | ASP232 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 402 |
Chain | Residue |
B | LEU122 |
B | GLN123 |
B | ASP155 |
B | HOH541 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CAC B 403 |
Chain | Residue |
A | HIS240 |
B | ILE68 |
B | GLU124 |
site_id | BC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE KGT B 404 |
Chain | Residue |
B | GLU45 |
B | HIS93 |
B | ASN110 |
B | LYS127 |
B | PHE131 |
B | GLU143 |
B | SER169 |
B | TYR170 |
B | ARG173 |
B | ALA194 |
B | PHE195 |
B | THR196 |
B | THR199 |
B | ARG250 |
B | HOH610 |
B | HOH611 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 401 |
Chain | Residue |
B | ALA202 |
B | HIS203 |
C | ARG209 |
C | TRP262 |
C | GLY263 |
C | LYS264 |
C | HOH574 |
C | HOH575 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL C 402 |
Chain | Residue |
C | THR76 |
C | GOL403 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL C 403 |
Chain | Residue |
C | GLN72 |
C | SER73 |
C | GOL402 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CAC C 404 |
Chain | Residue |
A | ARG7 |
A | LYS36 |
C | CYS14 |
C | MET227 |
site_id | BC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE KGT C 405 |
Chain | Residue |
C | GLU143 |
C | SER169 |
C | TYR170 |
C | ARG173 |
C | ALA194 |
C | PHE195 |
C | THR196 |
C | THR199 |
C | ARG250 |
C | GLU45 |
C | HIS93 |
C | ASN110 |
C | LYS127 |
C | PHE131 |
site_id | BC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL D 401 |
Chain | Residue |
A | ARG209 |
A | TRP262 |
A | GLY263 |
A | LYS264 |
A | HOH519 |
D | ALA202 |
D | HIS203 |
D | HOH547 |
site_id | BC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL D 402 |
Chain | Residue |
D | GLU124 |
D | TYR125 |
D | GLN126 |
D | LEU128 |
D | GLY150 |
D | LYS151 |
D | ALA152 |
D | PRO154 |
D | HOH530 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL D 403 |
Chain | Residue |
D | SER183 |
D | TRP298 |
D | ASP303 |
site_id | CC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CAC D 404 |
Chain | Residue |
D | ARG182 |
D | TRP298 |
site_id | CC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE KGT D 405 |
Chain | Residue |
D | GLU45 |
D | HIS93 |
D | ASN110 |
D | LYS127 |
D | PHE131 |
D | GLU143 |
D | SER169 |
D | TYR170 |
D | ARG173 |
D | ALA194 |
D | PHE195 |
D | THR196 |
D | THR199 |
D | ARG250 |
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 | SER169 | |
B | SER169 | |
C | SER169 | |
D | SER169 |
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 |