MolNFT v1 · #118502 · protein

Structure of oxidized udp-galactopyranose mutase from mycobacterium smegmatis in complex with magnesium ion

5F3R: “Structure of oxidized udp-galactopyranose mutase from mycobacterium smegmatis in complex with magnesium ion”. X-ray diffraction, 2 ligands (FAD, MG), 2 pockets (best druggability 0.81). MolNFT v1 #118502 on GenesisL1: 3D structure…

PDB: 5F3R
Type: protein
Length: 391 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Udp-galactopyranose mutase
EC: 5.4.99.9
UniProt: A0R629
Ligands: FAD, MG
Pockets: 2 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Udp-galactopyranose mutase (EC 5.4.99.9)	protein	391	39% helix, 19% strand	A0R629

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · chains A
MG · Magnesium ion · metal · chains A
DMS · Dimethyl sulfoxide · additive · 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	1096	0.81	0.82	92	FAD, DMS
2	153	0.47	0.77	23	empty

Compared structures

5F3R · Structure of oxidized UDP-galactopyranose mutase from Mycobacterium smegmatis in complex… · 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 A0R629
Elsewhere: RCSB PDB 5F3R · PDBe 5F3R · UniProt A0R629

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