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Crystal structure of P202 HIN1

Analyse Crystal structure of P202 HIN1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4L5Q
Type: protein
Length: 199 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Interferon-activable protein 202
UniProt: Q9R002
Pockets: 3 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Interferon-activable protein 202	protein	199	10% helix, 43% strand	Q9R002

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	201	0.47	0.75	34	empty
2	76	0.45	0.82	18	empty
3	90	0.41	0.77	16	empty

Compared structures

4L5Q · Crystal structure of p202 HIN1 · the same entry in another collection · chain A against A, TM-score 1.00
Q9R002 · AlphaFold monomer V2.0 prediction for interferon-activable protein 202 (Q9R002) · a predicted model of the same protein · chain A against A, TM-score 0.95

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9R002
Elsewhere: RCSB PDB 4L5Q · PDBe 4L5Q · UniProt Q9R002

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