6YVZ
HIF prolyl hydroxylase 2 (PHD2/ EGLN1) in complex with bicyclic JLS-367
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue MN A 501 |
Chain | Residue |
A | HIS313 |
A | ASP315 |
A | HIS374 |
A | PW8502 |
A | HOH617 |
site_id | AC2 |
Number of Residues | 16 |
Details | binding site for residue PW8 A 502 |
Chain | Residue |
A | TYR329 |
A | LEU343 |
A | HIS374 |
A | VAL376 |
A | ARG383 |
A | ARG398 |
A | VAL401 |
A | MN501 |
A | HOH617 |
A | HOH633 |
A | HOH641 |
A | HOH643 |
A | TYR310 |
A | HIS313 |
A | ASP315 |
A | ILE327 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue BCT A 503 |
Chain | Residue |
A | ARG312 |
A | PRO373 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16782814, ECO:0000269|PubMed:19604478, ECO:0000269|PubMed:28594552, ECO:0007744|PDB:2G19, ECO:0007744|PDB:3HQU, ECO:0007744|PDB:5V18 |
Chain | Residue | Details |
A | HIS313 | |
A | ASP315 | |
A | HIS374 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:19604478 |
Chain | Residue | Details |
A | ARG383 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:21601578 |
Chain | Residue | Details |
A | CYS201 | |
A | CYS208 | |
A | CYS302 | |
A | CYS323 | |
A | CYS326 |