MolNFT v1 · #93836 · protein

Crystal structure analysis of apo-groel structure

4HEL · 60 kda chaperonin 4: “Crystal structure analysis of apo-groel structure”. X-ray diffraction, 20 pockets (best druggability 0.82). MolNFT v1 #93836 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4HEL
Type: protein
Length: 7,350 residues
Chains: 14
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 60 kda chaperonin 4
UniProt: Q548M1
Pockets: 20 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N	60 kda chaperonin 4	protein	525	53% helix, 18% strand	Q548M1

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	1082	0.82	0.83	116	empty
2	1037	0.81	0.82	102	empty
3	883	0.81	0.83	96	empty
4	1128	0.80	0.81	114	empty
5	1114	0.80	0.81	95	empty

Interfaces

29 interfaces between chains.

M–N · 1899 Å² buried · 25 hydrogen bonds · protein-protein
E–F · 1828 Å² buried · 18 hydrogen bonds · protein-protein
A–G · 1818 Å² buried · 21 hydrogen bonds · protein-protein
H–N · 1813 Å² buried · 20 hydrogen bonds · protein-protein
L–M · 1811 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

4HEL · Crystal structure analysis of apo-GroEL structure · the same entry in another collection · chain A against A, 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 Q548M1
Elsewhere: RCSB PDB 4HEL · PDBe 4HEL · UniProt Q548M1

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