Research workbench

Human factor inhibiting hif (FIH1)

Analyse Human factor inhibiting hif (FIH1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MZE
Type: protein
Length: 335 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Factor inhibiting HIF1
UniProt: Q9NWT6
Ligands: FE2
Pockets: 5 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Factor inhibiting HIF1	protein	335	31% helix, 26% strand	Q9NWT6

Ligands and binding sites

FE2 · Fe (II) ion · metal · chains A
TAR · D(-)-tartaric acid · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	376	0.67	0.80	38	FE2, TAR
2	106	0.49	0.81	22	empty
3	133	0.42	0.75	24	empty
4	119	0.41	0.76	25	empty
5	97	0.38	0.76	17	empty

Compared structures

1MZE · Human Factor Inhibiting HIF (FIH1) · the same entry in another collection · chain A against A, TM-score 1.00
Q9NWT6 · AlphaFold monomer V2.0 prediction for hypoxia-inducible factor 1-alpha inhibitor (Q9NWT6) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q9NWT6
Elsewhere: RCSB PDB 1MZE · PDBe 1MZE · UniProt Q9NWT6

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