MolNFT v1 · #94739 · protein

Crystal structure of W-W-R clpx hexamer

4I5O · ATP-dependent clp protease ATP-binding subunit clpx: “Crystal structure of W-W-R clpx hexamer”. X-ray diffraction, 1 ligand (SO4), 18 pockets (best druggability 0.84). MolNFT v1 #94739 on GenesisL1: 3D structure, binding sites and…

PDB: 4I5O
Type: protein
Length: 1,866 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP-dependent clp protease ATP-binding subunit clpx
UniProt: P0A6H1
Ligands: SO4
Pockets: 18 · best druggability 0.84

Structure

x-ray diffraction · 6 distinct chains · 49% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATP-dependent clp protease ATP-binding subunit clpx	protein	309	49% helix, 11% strand	P0A6H1
B	ATP-dependent clp protease ATP-binding subunit clpx	protein	308	51% helix, 11% strand	P0A6H1
C	ATP-dependent clp protease ATP-binding subunit clpx	protein	317	48% helix, 11% strand	P0A6H1
D	ATP-dependent clp protease ATP-binding subunit clpx	protein	304	48% helix, 12% strand	P0A6H1
E	ATP-dependent clp protease ATP-binding subunit clpx	protein	318	49% helix, 11% strand	P0A6H1
F	ATP-dependent clp protease ATP-binding subunit clpx	protein	310	48% helix, 11% strand	P0A6H1

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A, B, C, D, E, F

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

Pockets

18 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	986	0.84	0.85	78	SO4
2	1139	0.83	0.84	105	SO4
3	1131	0.83	0.83	95	SO4
4	1106	0.82	0.83	88	SO4
5	1112	0.81	0.82	88	SO4

Interfaces

6 interfaces between chains.

C–D · 1326 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 1258 Å² buried · 9 hydrogen bonds · protein-protein
A–F · 1161 Å² buried · 9 hydrogen bonds · protein-protein
B–C · 1159 Å² buried · 6 hydrogen bonds · protein-protein
D–E · 1131 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

P0A6H1 · AlphaFold monomer V2.0 prediction for ATP-dependent clp protease ATP- binding subunit… · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P0A6H1
Elsewhere: RCSB PDB 4I5O · PDBe 4I5O · UniProt P0A6H1

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