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Crystal structure of kemp eliminase HG3.17 in the inactive state

Analyse Crystal structure of kemp eliminase HG3.17 in the inactive state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7K4W
Type: protein
Length: 286 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-beta-xylanase
EC: 3.2.1.8
UniProt: P23360
Ligands: CA
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-xylanase (EC 3.2.1.8)	protein	286	45% helix, 20% strand	P23360

Ligands and binding sites

CA · Calcium ion · metal · 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	123	0.61	0.86	32	empty
2	77	0.40	0.78	15	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

7K4W · Crystal structure of Kemp Eliminase HG3.17 in the inactive state · the same entry in another collection · chain A against A, TM-score 1.00
P23360 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase (P23360) · 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 P23360
Elsewhere: RCSB PDB 7K4W · PDBe 7K4W · UniProt P23360

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