MolNFT v1 · #118811 · protein

The high resolution structure of apo form dihydrofolate reductase from yersinia pestis at 1.55 a

5FDA: “The high resolution structure of apo form dihydrofolate reductase from yersinia pestis at 1.55 a”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.44). MolNFT v1 #118811 on GenesisL1: 3D structure, binding sites and…

PDB: 5FDA
Type: protein
Length: 161 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydrofolate reductase
EC: 1.5.1.3
UniProt: A0A0B6NYF5
Ligands: CL
Pockets: 2 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydrofolate reductase (EC 1.5.1.3)	protein	161	21% helix, 33% strand	A0A0B6NYF5

Ligands and binding sites

CL · Chloride ion · ion · 3 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	101	0.44	0.79	23	empty
2	65	0.30	0.75	15	empty

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

5FDA · The high resolution structure of apo form dihydrofolate reductase from Yersinia pestis at… · 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 A0A0B6NYF5
Elsewhere: RCSB PDB 5FDA · PDBe 5FDA · UniProt A0A0B6NYF5

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