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Crystal structure of TWHD1 of RPC5 subunit of human RNA polymerase III

Analyse Crystal structure of TWHD1 of RPC5 subunit of human RNA polymerase III in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ASU
Type: protein
Length: 169 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA-directed RNA polymerase III subunit RPC5
UniProt: Q9NVU0
Ligands: ZN
Pockets: 2 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 59% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA-directed RNA polymerase III subunit RPC5	protein	169	59% helix, 12% strand	Q9NVU0

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	93	0.38	0.75	17	ZN
2	77	0.33	0.75	16	ZN

Compared structures

7ASU · Crystal structure of tWHD1 of Rpc5 subunit of human RNA Polymerase III · the same entry in another collection · chain A against A, TM-score 1.00
Q9NVU0 · AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase III subunit RPC5… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q9NVU0
Elsewhere: RCSB PDB 7ASU · PDBe 7ASU · UniProt Q9NVU0

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