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Ensemble refinement of the protein crystal structure of gene product from homo sapiens HS.95870

Analyse Ensemble refinement of the protein crystal structure of gene product from homo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Q4Q
Type: protein
Length: 234 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: UPF0366 protein C11ORF67
UniProt: Q9H7C9
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	UPF0366 protein C11ORF67	protein	122	26% helix, 28% strand	Q9H7C9
B	UPF0366 protein C11ORF67	protein	112	29% helix, 25% strand	Q9H7C9

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	223	0.50	0.75	32	empty

Interfaces

1 interface between chains.

A–B · 278 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

2Q4Q · Ensemble refinement of the protein crystal structure of gene product from Homo sapiens… · the same entry in another collection · chain A against A, TM-score 1.00
Q9H7C9 · AlphaFold monomer V2.0 prediction for MTH938 domain-containing protein (Q9H7C9) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9H7C9
Elsewhere: RCSB PDB 2Q4Q · PDBe 2Q4Q · UniProt Q9H7C9

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