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Crystal structure of the K. lactis RAD5

Analyse Crystal structure of the K. lactis RAD5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6L8N
Type: protein
Length: 810 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA repair protein RAD5
EC: 3.6.4.-
UniProt: Q6CJM4
Ligands: ZN
Pockets: 10 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA repair protein RAD5 (EC 3.6.4.-)	protein	810	38% helix, 19% strand	Q6CJM4

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	328	0.69	0.83	41	empty
2	354	0.62	0.78	46	empty
3	319	0.56	0.76	38	empty
4	308	0.56	0.76	37	empty
5	177	0.45	0.75	34	empty

Compared structures

6L8N · Crystal structure of the K. lactis Rad5 · the same entry in another collection · chain A against A, TM-score 1.00
Q6CJM4 · AlphaFold monomer V2.0 prediction for DNA repair protein RAD5 (Q6CJM4) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q6CJM4
Elsewhere: RCSB PDB 6L8N · PDBe 6L8N · UniProt Q6CJM4

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