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Native structure of a family 35 carbohydrate binding module from clostridium thermocellum

Analyse Native structure of a family 35 carbohydrate binding module from clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2W1W
Type: protein
Length: 262 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipolytic enzyme, G-D-S-L
UniProt: A3DK57
Ligands: CA, PO4
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 2% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipolytic enzyme, G-D-S-L	protein	130	2% helix, 54% strand	A3DK57
B	Lipolytic enzyme, G-D-S-L	protein	132	2% helix, 58% strand	A3DK57

Ligands and binding sites

CA · Calcium ion · metal · 3 copies · chains A, B
PO4 · Phosphate ion · ion · chains B
GOL · Glycerol · additive · chains B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	79	0.38	0.78	18	empty

Interfaces

1 interface between chains.

A–B · 442 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2W1W · Native structure of a family 35 carbohydrate binding module from Clostridium thermocellum · 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 A3DK57
Elsewhere: RCSB PDB 2W1W · PDBe 2W1W · UniProt A3DK57

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