MolNFT v1 · #161729 · protein

Liquid application method for time-resolved analyses (lama) by serial synchrotron crystallography, xylose isomerase 0MS timepoint

6QNH: “Liquid application method for time-resolved analyses (lama) by serial synchrotron crystallography, xylose…”. X-ray diffraction, 2 ligands (MG, CO), 5 pockets (best druggability 0.74). MolNFT v1 #161729 on GenesisL1: 3D structure…

PDB: 6QNH
Type: protein
Length: 387 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylose isomerase
EC: 5.3.1.5
UniProt: P24300
Ligands: MG, CO
Pockets: 5 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xylose isomerase (EC 5.3.1.5)	protein	387	50% helix, 10% strand	P24300

Ligands and binding sites

MG · Magnesium ion · metal · chains A
CO · Cobalt (II) ion · metal · chains A

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	59	0.74	0.99	24	empty
2	500	0.67	0.78	46	empty
3	99	0.46	0.80	13	empty
4	59	0.35	0.78	12	empty
5	52	0.26	0.73	13	empty

Compared structures

6QNH · Liquid Application Method for time-resolved Analyses (LAMA) by serial synchrotron… · 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 P24300
Elsewhere: RCSB PDB 6QNH · PDBe 6QNH · UniProt P24300

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