MolNFT v1 · #186559 · protein

Aspergillus fumigatus enolase

7RHV: “Aspergillus fumigatus enolase”. X-ray diffraction, 1 ligand (MG), 6 pockets (best druggability 0.73). MolNFT v1 #186559 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7RHV
Type: protein
Length: 859 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enolase
EC: 4.2.1.11
UniProt: Q96X30
Ligands: MG
Pockets: 6 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enolase (EC 4.2.1.11)	protein	424	45% helix, 18% strand	Q96X30
B	Enolase (EC 4.2.1.11)	protein	435	45% helix, 17% strand	Q96X30

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1049	0.73	0.77	51	empty
2	391	0.60	0.77	54	empty
3	312	0.58	0.77	55	empty
4	91	0.38	0.76	16	empty
5	105	0.37	0.75	18	empty

Interfaces

1 interface between chains.

A–B · 1793 Å² buried · 35 hydrogen bonds · protein-protein

Compared structures

7RHV · Aspergillus fumigatus Enolase · the same entry in another collection · chain A against A, TM-score 1.00
Q96X30 · AlphaFold monomer V2.0 prediction for enolase (Q96X30) · a predicted model of the same protein · 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 Q96X30
Elsewhere: RCSB PDB 7RHV · PDBe 7RHV · UniProt Q96X30

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