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High resolution crystal structure of clpa

Analyse High resolution crystal structure of clpa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1R6B
Type: protein
Length: 704 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Clpa protein
UniProt: P0ABH9
Ligands: ADP, MG
Pockets: 10 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	Clpa protein	protein	704	50% helix, 13% strand	P0ABH9

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains X
MG · Magnesium ion · metal · 3 copies · chains X

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	384	0.64	0.78	36	empty
2	283	0.61	0.80	30	MG, ADP
3	299	0.59	0.78	37	empty
4	188	0.51	0.77	30	MG, ADP
5	107	0.38	0.75	23	empty

Compared structures

1R6B · High resolution crystal structure of ClpA · the same entry in another collection · chain X against X, TM-score 1.00
P0ABH9 · AlphaFold monomer V2.0 prediction for ATP-dependent clp protease ATP- binding subunit… · a predicted model of the same protein · chain X against A, TM-score 0.57

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 P0ABH9
Elsewhere: RCSB PDB 1R6B · PDBe 1R6B · UniProt P0ABH9

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