Research workbench
Hif prolyl hydroxylase 2 (PHD2/ EGLN1) in complex with MN(II) and 2- (4-hydroxy-2-oxo-1,2-dihydroquinoline-3-CARBOXAMIDO)ACETIC acid
Analyse Hif prolyl hydroxylase 2 (PHD2/ EGLN1) in complex with MN(II) and 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BQW
- Type
- protein
- Length
- 216 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Egl nine homolog 1
- EC
- 1.14.11.-
- UniProt
- Q9GZT9
- Ligands
- QNM, MN
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Egl nine homolog 1 (EC 1.14.11.-) | protein | 216 | 27% helix, 30% strand | Q9GZT9 |
Ligands and binding sites
- QNM · 2-[(1-methyl-2-oxidanyl-4-oxidanylidene-quinolin-3-yl)carbonylamino]ethanoic acid · ligand · chains A
- MN · Manganese (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.66 | 0.88 | 23 | MN, QNM |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9GZT9
- Elsewhere: RCSB PDB 4BQW · PDBe 4BQW · UniProt Q9GZT9
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