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The crystal structure of the udp-N-acetylenolpyruvoylglucosamine reductase from the vibrio cholerae O1 biovar tor

Analyse The crystal structure of the udp-N-acetylenolpyruvoylglucosamine reductase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3I99
Type: protein
Length: 340 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-N-acetylenolpyruvoylglucosamine reductase
EC: 1.1.1.158
UniProt: C3LQS2
Ligands: FAD, PO4
Pockets: 2 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-N-acetylenolpyruvoylglucosamine reductase (EC 1.1.1.158)	protein	340	27% helix, 29% strand	C3LQS2

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
PO4 · Phosphate ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1042	0.82	0.83	99	FAD, PO4
2	54	0.30	0.75	12	empty

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

3I99 · The crystal structure of the UDP-N-acetylenolpyruvoylglucosamine reductase from the… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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Every structure of UniProt C3LQS2
Elsewhere: RCSB PDB 3I99 · PDBe 3I99 · UniProt C3LQS2

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