Research workbench

X-ray crystal structure of S. cerevisiae CGI121

Analyse X-ray crystal structure of S. cerevisiae CGI121 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4XAH
Type: protein
Length: 355 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: EKC/KEOPS complex subunit CGI121
UniProt: Q03705
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	EKC/KEOPS complex subunit CGI121	protein	177	47% helix, 14% strand	Q03705
B	EKC/KEOPS complex subunit CGI121	protein	178	46% helix, 17% strand	Q03705

Pockets

2 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	493	0.64	0.77	48	empty
2	77	0.42	0.80	16	empty

Interfaces

1 interface between chains.

A–B · 447 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (artifact).

Compared structures

4XAH · X-ray crystal structure of S. cerevisiae Cgi121 · the same entry in another collection · chain A against A, TM-score 1.00
Q03705 · AlphaFold monomer V2.0 prediction for EKC/KEOPS complex subunit CGI121 (Q03705) · a predicted model of the same protein · chain B 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 Q03705
Elsewhere: RCSB PDB 4XAH · PDBe 4XAH · UniProt Q03705

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