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Structure of the bottromycin epimerase both in complex with bottromycin A2 derivative

Analyse Structure of the bottromycin epimerase both in complex with bottromycin A2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6T70
Type: protein
Length: 253 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Both
UniProt: K4MHV9
Ligands: MQZ, ZN, CL, SO4
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Both	protein	253	43% helix, 19% strand	K4MHV9

Ligands and binding sites

MQZ · Bottromycin A2 derivative · ligand · chains A
ZN · Zinc ion · metal · chains A
CL · Chloride ion · ion · chains A
SO4 · Sulfate ion · ion · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	540	0.70	0.79	30	CL, MQZ

Compared structures

6T70 · Structure of the Bottromycin epimerase BotH in complex with Bottromycin A2 derivative · 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 K4MHV9
Elsewhere: RCSB PDB 6T70 · PDBe 6T70 · UniProt K4MHV9

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