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Crystal structure of enolase AGR_L_2751 from agrobacterium tumefaciens

Analyse Crystal structure of enolase AGR_L_2751 from agrobacterium tumefaciens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RVK
Type: protein
Length: 381 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ISOMERASE/LACTONIZING enzyme
UniProt: Q8UAC1
Ligands: MG
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ISOMERASE/LACTONIZING enzyme	protein	381	39% helix, 23% strand	Q8UAC1

Ligands and binding sites

MG · Magnesium ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	965	0.76	0.79	77	empty

Modifications

Observed in the structure: 11 modified (engineered).

Compared structures

1RVK · Crystal structure of enolase AGR_L_2751 from Agrobacterium Tumefaciens · 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 Q8UAC1
Elsewhere: RCSB PDB 1RVK · PDBe 1RVK · UniProt Q8UAC1

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