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Transcriptional repressor copg

Analyse Transcriptional repressor copg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CPG
Type: protein
Length: 130 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcriptional repressor copg
UniProt: P13920
Ligands: CL
Pockets: 1 · best druggability 0.46

Structure

x-ray diffraction · 3 distinct chains · 65% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcriptional repressor copg	protein	43	65% helix, 21% strand	P13920
B	Transcriptional repressor copg	protein	45	67% helix, 20% strand	P13920
C	Transcriptional repressor copg	protein	42	64% helix, 0% strand	P13920

Ligands and binding sites

CL · Chloride ion · ion · 3 copies · chains A, B, C

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

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	130	0.46	0.77	22	empty

Interfaces

3 interfaces between chains.

A–B · 1701 Å² buried · 22 hydrogen bonds · protein-protein
B–C · 346 Å² buried · 2 hydrogen bonds · protein-protein
A–C · 113 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

2CPG · Transcriptional repressor copg · the same entry in another collection · chain B against B, TM-score 1.00
P13920 · AlphaFold monomer V2.0 prediction for protein copg (P13920) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 P13920
Elsewhere: RCSB PDB 2CPG · PDBe 2CPG · UniProt P13920

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