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Crystal structure of T. maritima uvra D117-399 with ADP

Analyse Crystal structure of T. maritima uvra D117-399 with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6N9L
Type: protein
Length: 625 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uvrabc system protein a
UniProt: Q9WYV0
Ligands: ADP, ZN
Pockets: 4 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uvrabc system protein a	protein	625	39% helix, 18% strand	Q9WYV0

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A
ZN · Zinc ion · metal · chains A

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

Pockets

4 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	1062	0.75	0.78	104	ADP
2	254	0.70	0.86	36	empty
3	54	0.40	0.81	11	empty
4	77	0.38	0.78	17	empty

Compared structures

6N9L · Crystal structure of T. maritima UvrA d117-399 with ADP · the same entry in another collection · chain A against A, TM-score 1.00
Q9WYV0 · AlphaFold monomer V2.0 prediction for uvrabc system protein a (Q9WYV0) · 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 Q9WYV0
Elsewhere: RCSB PDB 6N9L · PDBe 6N9L · UniProt Q9WYV0

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