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Crystal structure of ligand-free bifunctional folylpolyglutamate SYNTHASE/DIHYDROFOLATE synthase from yersinia pestis C092

Analyse Crystal structure of ligand-free bifunctional folylpolyglutamate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NRS
Type: protein
Length: 401 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DIHYDROFOLATE:FOLYLPOLYGLUTAMATE synthetase
UniProt: Q8D0U0
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DIHYDROFOLATE:FOLYLPOLYGLUTAMATE synthetase	protein	401	40% helix, 19% strand	Q8D0U0

Ligands and binding sites

TLA · L(+)-tartaric acid · additive · 3 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	715	0.74	0.80	70	TLA, GOL, MES
2	135	0.51	0.80	31	empty
3	94	0.39	0.76	18	empty

Compared structures

3NRS · Crystal structure of ligand-free bifunctional folylpolyglutamate synthase/dihydrofolate… · 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 Q8D0U0
Elsewhere: RCSB PDB 3NRS · PDBe 3NRS · UniProt Q8D0U0

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