MolNFT v1 · #17007 · protein

Purification, crystallisation and preliminary structural studies of dtdp-4-keto-6-deoxy-glucose-5-epimerase (evad) from amycolatopsis orientalis; the fourth enzyme in the dtdp-L-epivancosamine biosynthetic pathway.

1OFN · PCZA361.16: “Purification, crystallisation and preliminary structural studies of dtdp-4-keto-6-deoxy-glucose-5-epimerase…”. X-ray diffraction, 4 pockets (best druggability 0.72). MolNFT v1 #17007 on GenesisL1: 3D structure, binding…

PDB: 1OFN
Type: protein
Length: 404 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PCZA361.16
UniProt: O52806
Pockets: 4 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	PCZA361.16	protein	202	16% helix, 36% strand	O52806

Ligands and binding sites

GOL · Glycerol · additive · 4 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.72	0.98	21	GOL
2	229	0.65	0.83	30	empty
3	223	0.64	0.83	28	GOL
4	51	0.25	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 1773 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

1OFN · Purification, crystallisation and preliminary structural studies of… · 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 O52806
Elsewhere: RCSB PDB 1OFN · PDBe 1OFN · UniProt O52806

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