MolNFT v1 · #75725 · protein

Crystal structure of bifunctional folylpolyglutamate SYNTHASE/DIHYDROFOLATE synthase complexed with amppnp and mn ion from yersinia pestis C092

3PYZ: “Crystal structure of bifunctional folylpolyglutamate SYNTHASE/DIHYDROFOLATE synthase complexed with amppnp…”. X-ray diffraction, 2 ligands (ANP, MN), 2 pockets (best druggability 0.75). MolNFT v1 #75725 on GenesisL1: 3D structure…

PDB: 3PYZ
Type: protein
Length: 410 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bifunctional folylpolyglutamate SYNTHASE/DIHYDROFOLATE synthase
EC: 6.3.2.12, 6.3.2.17
UniProt: Q1CHM3
Ligands: ANP, MN
Pockets: 2 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional folylpolyglutamate SYNTHASE/DIHYDROFOLATE synthase (EC 6.3.2.12, 6.3.2.17)	protein	410	39% helix, 18% strand	Q1CHM3

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
MN · Manganese (II) ion · metal · 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	782	0.75	0.79	84	ANP, MN
2	136	0.48	0.79	26	empty

Compared structures

3PYZ · Crystal structure of bifunctional folylpolyglutamate synthase/dihydrofolate synthase… · 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 Q1CHM3
Elsewhere: RCSB PDB 3PYZ · PDBe 3PYZ · UniProt Q1CHM3

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