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Crystal structure of the catalytic domain of licms in complexed with pyruvate

Analyse Crystal structure of the catalytic domain of licms in complexed with pyruvate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BLF
Type: protein
Length: 306 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Citramalate synthase from leptospira interrogans
EC: 2.3.3.13
UniProt: Q8F3Q1
Ligands: PYR, ZN
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Citramalate synthase from leptospira interrogans (EC 2.3.3.13)	protein	306	47% helix, 14% strand	Q8F3Q1

Ligands and binding sites

PYR · Pyruvic acid · ligand · chains A
ZN · Zinc 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	85	0.47	0.81	14	ZN, PYR

Compared structures

3BLF · Crystal structure of the catalytic domain of LiCMS in complexed with pyruvate · the same entry in another collection · chain A against A, TM-score 1.00
Q8F3Q1 · AlphaFold monomer V2.0 prediction for (R)-citramalate synthase cima (Q8F3Q1) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q8F3Q1
Elsewhere: RCSB PDB 3BLF · PDBe 3BLF · UniProt Q8F3Q1

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