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Crystal structure of the enolpyruvyl transferase niko from streptomyces tendae

Analyse Crystal structure of the enolpyruvyl transferase niko from streptomyces tendae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FQD
Type: protein
Length: 871 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Niko protein
UniProt: Q712I1
Ligands: SO4
Pockets: 8 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Niko protein	protein	436	34% helix, 27% strand	Q712I1
B	Niko protein	protein	435	36% helix, 27% strand	Q712I1

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	291	0.74	0.87	44	SO4
2	353	0.70	0.83	37	SO4
3	305	0.57	0.77	31	empty
4	294	0.56	0.76	35	empty
5	118	0.46	0.78	27	empty

Interfaces

1 interface between chains.

A–B · 986 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

4FQD · Crystal structure of the enolpyruvyl transferase NikO from Streptomyces tendae · 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 Q712I1
Elsewhere: RCSB PDB 4FQD · PDBe 4FQD · UniProt Q712I1

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