MolNFT v1 · #174075 · protein

Glucose isomerase S171W in H32

7BJZ · Xylose isomerase: “Glucose isomerase S171W in H32”. X-ray diffraction, 1 ligand (MN), 9 pockets (best druggability 0.82). MolNFT v1 #174075 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7BJZ
Type: protein
Length: 772 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylose isomerase
EC: 5.3.1.5
UniProt: P24300
Ligands: MN
Pockets: 9 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Xylose isomerase (EC 5.3.1.5)	protein	386	49% helix, 10% strand	P24300

Ligands and binding sites

MN · Manganese (II) ion · metal · 4 copies · chains A, B

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

Pockets

9 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	228	0.82	0.95	42	empty
2	370	0.70	0.82	42	MN
3	385	0.70	0.82	48	MN
4	91	0.51	0.83	14	empty
5	85	0.49	0.82	14	empty

Interfaces

1 interface between chains.

A–B · 1594 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

7BJZ · GLUCOSE ISOMERASE S171W in H32 · 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 7BJZ · PDBe 7BJZ · UniProt P24300

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