1EMS
CRYSTAL STRUCTURE OF THE C. ELEGANS NITFHIT PROTEIN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005575 | cellular_component | cellular_component |
| A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| 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 | 0047710 | molecular_function | bis(5'-adenosyl)-triphosphatase activity |
| A | 0110050 | molecular_function | deaminated glutathione amidase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005575 | cellular_component | cellular_component |
| B | 0006139 | biological_process | nucleobase-containing compound metabolic process |
| 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 | 0047710 | molecular_function | bis(5'-adenosyl)-triphosphatase activity |
| B | 0110050 | molecular_function | deaminated glutathione amidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EMC A 451 |
| Chain | Residue |
| A | GLU54 |
| A | LYS127 |
| A | GLU143 |
| A | CYS169 |
| A | ALA194 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EMC B 452 |
| Chain | Residue |
| B | ALA194 |
| B | GLU54 |
| B | LYS127 |
| B | GLU143 |
| B | CYS169 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EMC A 453 |
| Chain | Residue |
| A | CYS55 |
| A | GLY96 |
| A | HIS98 |
| A | ASN110 |
| A | SER147 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EMC A 454 |
| Chain | Residue |
| A | CYS75 |
| A | PHE304 |
| A | VAL388 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EMC B 455 |
| Chain | Residue |
| B | CYS55 |
| B | GLY96 |
| B | LEU97 |
| B | HIS98 |
| B | ASN110 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 456 |
| Chain | Residue |
| A | TYR218 |
| A | HOH531 |
| B | SER252 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 457 |
| Chain | Residue |
| A | SER167 |
| A | SER178 |
| A | ASN181 |
| A | LEU189 |
| A | HOH561 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 458 |
| Chain | Residue |
| B | MET71 |
| B | CYS75 |
| B | GLU76 |
| B | TYR77 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 459 |
| Chain | Residue |
| A | CYS377 |
| A | GLN379 |
| A | HIS394 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD A 502 |
| Chain | Residue |
| A | GLU253 |
| B | MET273 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: ACT_SITE => ECO:0000303|PubMed:9671749 |
| Chain | Residue | Details |
| A | GLU54 | |
| A | LYS127 | |
| A | CYS169 | |
| B | GLU54 | |
| B | LYS127 | |
| B | CYS169 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Tele-AMP-histidine intermediate => ECO:0000250|UniProtKB:P49789, ECO:0000255|PROSITE-ProRule:PRU00054 |
| Chain | Residue | Details |
| A | HIS392 | |
| B | HIS392 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 5fit |
| Chain | Residue | Details |
| A | HIS392 | |
| A | GLN379 | |
| A | HIS390 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 5fit |
| Chain | Residue | Details |
| B | HIS392 | |
| B | GLN379 | |
| B | HIS390 |
