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Crystal structure of clpp from staphylococcus aureus in the active, extended conformation

Analyse Crystal structure of clpp from staphylococcus aureus in the active, extended… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3V5E
Type: protein
Length: 2,576 residues
Chains: 14
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP-dependent clp protease proteolytic subunit
EC: 3.4.21.92
UniProt: Q2G036
Pockets: 20 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N	ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92)	protein	184	45% helix, 26% strand	Q2G036

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	336	0.64	0.79	54	empty
2	338	0.63	0.79	60	empty
3	344	0.61	0.78	51	empty
4	285	0.61	0.79	51	empty
5	325	0.61	0.78	55	empty

Interfaces

35 interfaces between chains.

M–N · 1656 Å² buried · 12 hydrogen bonds · protein-protein
H–N · 1653 Å² buried · 15 hydrogen bonds · protein-protein
D–E · 1652 Å² buried · 14 hydrogen bonds · protein-protein
J–K · 1645 Å² buried · 14 hydrogen bonds · protein-protein
K–L · 1644 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

3V5E · Crystal structure of ClpP from Staphylococcus aureus in the active, extended conformation · the same entry in another collection · chain K against K, TM-score 1.00

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 Q2G036
Elsewhere: RCSB PDB 3V5E · PDBe 3V5E · UniProt Q2G036

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