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Replication Factor C ADPNP complex

Analyse Replication Factor C ADPNP complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CHQ
Type: protein
Length: 939 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.5
Source: ARCHAEOGLOBUS FULGIDUS
Molecule: Replication factor C small subunit
UniProt: O28219
Ligands: ANP
Pockets: 8 · best druggability 0.81

Structure

x-ray diffraction · resolution 3.5 · 1 distinct chain · 53% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Replication factor C small subunit	protein	313	53% helix, 9% strand	O28219

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 3 copies · chains A, B, C

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	850	0.81	0.84	85	ANP
2	911	0.77	0.80	83	empty
3	657	0.73	0.80	55	ANP
4	129	0.71	0.91	29	empty
5	235	0.69	0.85	29	ANP

Interfaces

2 interfaces between chains.

A–B · 1587 Å² buried · 20 hydrogen bonds · protein-protein
B–C · 1414 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

2CHQ · Replication factor C adpnp complex · the same entry in another collection · chain A against A, TM-score 1.00
O28219 · AlphaFold monomer V2.0 prediction for replication factor C small subunit (O28219) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 O28219
Elsewhere: RCSB PDB 2CHQ · PDBe 2CHQ · UniProt O28219

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