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Structure of human RPC62 (partial)

Analyse Structure of human RPC62 (partial) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XV4
Type: protein
Length: 399 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA-directed RNA polymerase III subunit RPC3
UniProt: Q9BUI4
Ligands: PO4
Pockets: 5 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 68% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
S	DNA-directed RNA polymerase III subunit RPC3	protein	399	68% helix, 7% strand	Q9BUI4

Ligands and binding sites

PO4 · Phosphate ion · ion · 3 copies · chains S

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	196	0.70	0.87	28	empty
2	559	0.65	0.76	62	PO4
3	85	0.39	0.77	10	empty
4	70	0.35	0.77	18	PO4
5	81	0.32	0.73	12	empty

Compared structures

2XV4 · Structure of Human RPC62 (partial) · the same entry in another collection · chain S against S, TM-score 1.00
Q9BUI4 · AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase III subunit RPC3… · a predicted model of the same protein · chain S 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 Q9BUI4
Elsewhere: RCSB PDB 2XV4 · PDBe 2XV4 · UniProt Q9BUI4

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