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Structure of human enolase 2 in complex with SF2312

Analyse Structure of human enolase 2 in complex with SF2312 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ZCW
Type: protein
Length: 866 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gamma-enolase
EC: 4.2.1.11
UniProt: P09104
Ligands: 4NG, MG
Pockets: 8 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Gamma-enolase (EC 4.2.1.11)	protein	433	43% helix, 17% strand	P09104

Ligands and binding sites

4NG · [(3S,5S)-1,5-dihydroxy-2-oxopyrrolidin-3-yl]phosphonic acid · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 4 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1066	0.74	0.77	59	empty
2	57	0.66	0.95	18	empty
3	297	0.65	0.81	47	empty
4	85	0.54	0.86	24	empty
5	201	0.54	0.78	30	empty

Interfaces

1 interface between chains.

A–B · 1997 Å² buried · 42 hydrogen bonds · protein-protein

Compared structures

4ZCW · Structure of Human Enolase 2 in complex with SF2312 · the same entry in another collection · chain A against A, TM-score 1.00
P09104 · AlphaFold monomer V2.0 prediction for gamma-enolase (P09104) · a predicted model of the same protein · chain B 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 P09104
Elsewhere: RCSB PDB 4ZCW · PDBe 4ZCW · UniProt P09104

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