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Imisx-ep of hg-baca soaking sad

Analyse Imisx-ep of hg-baca soaking sad in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FMT
Type: protein
Length: 254 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Undecaprenyl-diphosphatase
EC: 3.6.1.27
UniProt: P60933
Ligands: HG
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Undecaprenyl-diphosphatase (EC 3.6.1.27)	protein	254	76% helix, 1% strand	P60933

Ligands and binding sites

HG · Mercury (II) ion · metal · chains A
OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 4 copies · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 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	804	0.76	0.80	59	empty
2	51	0.30	0.75	11	empty

Compared structures

6FMT · IMISX-EP of Hg-BacA Soaking SAD · the same entry in another collection · chain A against A, TM-score 1.00
P60933 · AlphaFold monomer V2.0 prediction for undecaprenyl-diphosphatase (P60933) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P60933
Elsewhere: RCSB PDB 6FMT · PDBe 6FMT · UniProt P60933

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