Research workbench

AFGH61B L90V/D131S/M134L/A141W variant

Analyse AFGH61B L90V/D131S/M134L/A141W variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6HA5
Type: protein
Length: 456 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoglucanase, putative
EC: 3.2.1.-
UniProt: Q4WP32
Ligands: CU
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Endoglucanase, putative (EC 3.2.1.-)	protein	228	11% helix, 34% strand	Q4WP32

Ligands and binding sites

CU · Copper (II) ion · metal · 2 copies · chains A, B
ACT · Acetate ion · additive · 4 copies · chains A, B

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	574	0.69	0.78	55	ACT
2	175	0.47	0.76	24	ACT

Interfaces

1 interface between chains.

A–B · 318 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 2 modified (disulfide, methylation).

Compared structures

6HA5 · AFGH61B L90V/D131S/M134L/A141W variant · 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 Q4WP32
Elsewhere: RCSB PDB 6HA5 · PDBe 6HA5 · UniProt Q4WP32

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