6I7G
Crystal structure of dimeric wild type FICD complexed with ATP
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue ATP A 501 |
| Chain | Residue |
| A | GLU234 |
| A | ARG374 |
| A | TYR399 |
| A | TYR400 |
| A | LEU403 |
| A | ASN407 |
| A | HOH601 |
| A | HOH602 |
| A | HOH605 |
| A | HOH614 |
| A | VAL316 |
| A | HIS319 |
| A | VAL360 |
| A | HIS363 |
| A | GLY368 |
| A | ASN369 |
| A | GLY370 |
| A | ARG371 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 502 |
| Chain | Residue |
| A | TYR361 |
| A | ALA406 |
| A | 1PE503 |
| A | HOH619 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue 1PE A 503 |
| Chain | Residue |
| A | LYS358 |
| A | TYR361 |
| A | PEG502 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | binding site for residue ATP B 501 |
| Chain | Residue |
| B | GLU234 |
| B | HIS319 |
| B | VAL360 |
| B | HIS363 |
| B | GLY368 |
| B | ASN369 |
| B | GLY370 |
| B | ARG371 |
| B | ARG374 |
| B | TYR399 |
| B | TYR400 |
| B | LEU403 |
| B | ASN407 |
| B | HOH602 |
| B | HOH605 |
| B | HOH610 |
| B | HOH618 |
| B | HOH636 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue PG4 B 502 |
| Chain | Residue |
| B | LYS358 |
| B | GLY409 |
| B | 1PE503 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue 1PE B 503 |
| Chain | Residue |
| B | TRP337 |
| B | LYS358 |
| B | TYR361 |
| B | PG4502 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:22266942 |
| Chain | Residue | Details |
| A | HIS363 | |
| B | HIS363 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0U |
| Chain | Residue | Details |
| A | GLU234 | |
| B | GLU234 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0S, ECO:0007744|PDB:4U0U |
| Chain | Residue | Details |
| A | VAL316 | |
| A | TYR399 | |
| A | ASN407 | |
| B | VAL316 | |
| B | TYR399 | |
| B | ASN407 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07 |
| Chain | Residue | Details |
| A | ASP367 | |
| B | ASP367 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Important for autoinhibition of adenylyltransferase activity => ECO:0000269|PubMed:22266942, ECO:0000269|PubMed:25435325 |
| Chain | Residue | Details |
| A | GLU234 | |
| B | GLU234 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: O-AMP-threonine; by autocatalysis => ECO:0000305|PubMed:25601083 |
| Chain | Residue | Details |
| A | THR183 | |
| B | THR183 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:25601083 |
| Chain | Residue | Details |
| A | ASN275 | |
| B | ASN275 |
