6YVT
HIF prolyl hydroxylase 2 (PHD2/ EGLN1) in complex with MD-253
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005506 | molecular_function | iron ion binding |
A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
A | 0031418 | molecular_function | L-ascorbic acid binding |
B | 0005506 | molecular_function | iron ion binding |
B | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
B | 0031418 | molecular_function | L-ascorbic acid binding |
C | 0005506 | molecular_function | iron ion binding |
C | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
C | 0031418 | molecular_function | L-ascorbic acid binding |
D | 0005506 | molecular_function | iron ion binding |
D | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
D | 0031418 | molecular_function | L-ascorbic acid binding |
E | 0005506 | molecular_function | iron ion binding |
E | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
E | 0031418 | molecular_function | L-ascorbic acid binding |
F | 0005506 | molecular_function | iron ion binding |
F | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
F | 0031418 | molecular_function | L-ascorbic acid binding |
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 | PW2502 |
A | HOH605 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue PW2 A 502 |
Chain | Residue |
A | TYR329 |
A | LEU343 |
A | HIS374 |
A | VAL376 |
A | ARG383 |
A | MN501 |
A | HOH605 |
C | LYS400 |
C | VAL401 |
A | TYR303 |
A | TYR310 |
A | HIS313 |
A | ASP315 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue MN B 501 |
Chain | Residue |
B | HIS313 |
B | ASP315 |
B | HIS374 |
B | PW2502 |
B | HOH607 |
site_id | AC4 |
Number of Residues | 14 |
Details | binding site for residue PW2 B 502 |
Chain | Residue |
B | ILE251 |
B | ARG252 |
B | MET299 |
B | TYR303 |
B | HIS313 |
B | TYR329 |
B | LEU343 |
B | HIS374 |
B | VAL376 |
B | ARG383 |
B | MN501 |
B | HOH601 |
B | HOH607 |
F | VAL401 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue MN C 501 |
Chain | Residue |
C | HIS313 |
C | ASP315 |
C | HIS374 |
C | PW2502 |
C | HOH607 |
site_id | AC6 |
Number of Residues | 13 |
Details | binding site for residue PW2 C 502 |
Chain | Residue |
C | MET299 |
C | TYR303 |
C | TYR310 |
C | HIS313 |
C | ILE327 |
C | TYR329 |
C | HIS374 |
C | VAL376 |
C | ARG383 |
C | MN501 |
C | HOH607 |
D | VAL401 |
D | LEU404 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue MN D 501 |
Chain | Residue |
D | HIS313 |
D | ASP315 |
D | HIS374 |
D | PW2502 |
D | HOH606 |
site_id | AC8 |
Number of Residues | 16 |
Details | binding site for residue PW2 D 502 |
Chain | Residue |
A | LYS400 |
A | VAL401 |
D | ASP250 |
D | ARG252 |
D | MET299 |
D | TYR303 |
D | TYR310 |
D | HIS313 |
D | TYR329 |
D | LEU343 |
D | HIS374 |
D | VAL376 |
D | ARG383 |
D | MN501 |
D | HOH606 |
D | HOH607 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue MN E 501 |
Chain | Residue |
E | HIS313 |
E | ASP315 |
E | HIS374 |
E | PW2502 |
E | HOH609 |
site_id | AD1 |
Number of Residues | 12 |
Details | binding site for residue PW2 E 502 |
Chain | Residue |
B | VAL401 |
E | MET299 |
E | TYR303 |
E | HIS313 |
E | TYR329 |
E | LEU343 |
E | HIS374 |
E | VAL376 |
E | ARG383 |
E | MN501 |
E | HOH605 |
E | HOH609 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue GOL E 503 |
Chain | Residue |
E | VAL210 |
E | ASP211 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue SO4 E 504 |
Chain | Residue |
E | ASP355 |
E | GLU357 |
E | LYS359 |
E | ARG362 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue MN F 501 |
Chain | Residue |
F | HIS313 |
F | ASP315 |
F | HIS374 |
F | PW2502 |
F | HOH605 |
site_id | AD5 |
Number of Residues | 10 |
Details | binding site for residue PW2 F 502 |
Chain | Residue |
E | LYS400 |
F | TYR303 |
F | HIS313 |
F | TYR329 |
F | LEU343 |
F | HIS374 |
F | VAL376 |
F | ARG383 |
F | MN501 |
F | HOH605 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 18 |
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 | |
D | HIS313 | |
D | ASP315 | |
D | HIS374 | |
E | HIS313 | |
E | ASP315 | |
E | HIS374 | |
F | HIS313 | |
F | ASP315 | |
F | HIS374 | |
A | ASP315 | |
A | HIS374 | |
B | HIS313 | |
B | ASP315 | |
B | HIS374 | |
C | HIS313 | |
C | ASP315 | |
C | HIS374 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:19604478 |
Chain | Residue | Details |
A | ARG383 | |
B | ARG383 | |
C | ARG383 | |
D | ARG383 | |
E | ARG383 | |
F | ARG383 |
site_id | SWS_FT_FI3 |
Number of Residues | 30 |
Details | MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:21601578 |
Chain | Residue | Details |
A | CYS201 | |
B | CYS326 | |
C | CYS201 | |
C | CYS208 | |
C | CYS302 | |
C | CYS323 | |
C | CYS326 | |
D | CYS201 | |
D | CYS208 | |
D | CYS302 | |
D | CYS323 | |
A | CYS208 | |
D | CYS326 | |
E | CYS201 | |
E | CYS208 | |
E | CYS302 | |
E | CYS323 | |
E | CYS326 | |
F | CYS201 | |
F | CYS208 | |
F | CYS302 | |
F | CYS323 | |
A | CYS302 | |
F | CYS326 | |
A | CYS323 | |
A | CYS326 | |
B | CYS201 | |
B | CYS208 | |
B | CYS302 | |
B | CYS323 |