MolNFT v1 · #175401 · protein

Xylanase R from bacillus sp. tar-1

7CPK · Endo-1,4-beta-xylanase a: “Xylanase R from bacillus sp. tar-1”. X-ray diffraction, 2 ligands (CA, NI), 2 pockets (best druggability 0.53). MolNFT v1 #175401 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7CPK
Type: protein
Length: 357 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-beta-xylanase a
EC: 3.2.1.8
UniProt: P07528
Ligands: CA, NI
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-xylanase a (EC 3.2.1.8)	protein	357	45% helix, 17% strand	P07528

Ligands and binding sites

CA · Calcium ion · metal · 3 copies · chains A
NI · Nickel (II) ion · metal · 2 copies · chains A
MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · 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	155	0.53	0.80	28	empty
2	62	0.34	0.77	16	empty

Compared structures

7CPK · Xylanase R from Bacillus sp. TAR-1 · the same entry in another collection · chain A against A, TM-score 1.00
P07528 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase a (P07528) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P07528
Elsewhere: RCSB PDB 7CPK · PDBe 7CPK · UniProt P07528

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.