MolNFT v1 · #151093 · protein

Obp chaperonin in the nucleotide-free state

6HDD · Putative chaperonin groel: “Obp chaperonin in the nucleotide-free state”. Electron microscopy, 20 pockets (best druggability 0.81). MolNFT v1 #151093 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6HDD
Type: protein
Length: 3,605 residues
Chains: 7
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative chaperonin groel
UniProt: G9I9H9
Pockets: 20 · best druggability 0.81

Structure

electron microscopy · 1 distinct chain · 33% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G	Putative chaperonin groel	protein	515	33% helix, 9% strand	G9I9H9

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	525	0.81	0.88	59	empty
2	131	0.80	0.97	34	empty
3	985	0.79	0.81	90	empty
4	1196	0.79	0.81	117	empty
5	105	0.77	0.97	31	empty

Interfaces

7 interfaces between chains.

C–D · 1841 Å² buried · 20 hydrogen bonds · protein-protein
F–G · 1731 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 1664 Å² buried · 15 hydrogen bonds · protein-protein
E–F · 1501 Å² buried · 16 hydrogen bonds · protein-protein
A–G · 1489 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

6HDD · OBP chaperonin in the nucleotide-free state · 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 G9I9H9
Elsewhere: RCSB PDB 6HDD · PDBe 6HDD · UniProt G9I9H9

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