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Crystal structure of the tetrameric P202 HIN2

Analyse Crystal structure of the tetrameric P202 HIN2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4L5T
Type: protein
Length: 730 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Interferon-activable protein 202
UniProt: Q9R002
Pockets: 8 · best druggability 0.81

Structure

x-ray diffraction · 4 distinct chains · 9% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Interferon-activable protein 202	protein	180	12% helix, 52% strand	Q9R002
B	Interferon-activable protein 202	protein	185	8% helix, 51% strand	Q9R002
C	Interferon-activable protein 202	protein	182	9% helix, 53% strand	Q9R002
D	Interferon-activable protein 202	protein	183	9% helix, 51% strand	Q9R002

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	487	0.81	0.88	71	empty
2	548	0.71	0.80	62	empty
3	495	0.70	0.81	57	empty
4	301	0.67	0.83	33	empty
5	371	0.67	0.80	47	empty

Interfaces

6 interfaces between chains.

A–D · 1793 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 1791 Å² buried · 31 hydrogen bonds · protein-protein
A–C · 544 Å² buried · 2 hydrogen bonds · protein-protein
B–D · 431 Å² buried · 1 hydrogen bond · protein-protein
A–B · 251 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

4L5T · Crystal structure of the tetrameric p202 HIN2 · the same entry in another collection · chain D against D, TM-score 1.00
Q9R002 · AlphaFold monomer V2.0 prediction for interferon-activable protein 202 (Q9R002) · a predicted model of the same protein · chain D against A, TM-score 0.92

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 Q9R002
Elsewhere: RCSB PDB 4L5T · PDBe 4L5T · UniProt Q9R002

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