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Structure of FAM17 carbohydrate binding module from clostridium cellulovorans

Analyse Structure of FAM17 carbohydrate binding module from clostridium cellulovorans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1J83
Type: protein
Length: 360 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-beta glucanase engf
EC: 3.2.1.4
UniProt: P94622
Ligands: CA
Pockets: 2 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Endo-1,4-beta glucanase engf (EC 3.2.1.4)	protein	180	7% helix, 39% strand	P94622

Ligands and binding sites

CA · Calcium ion · metal · 2 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	261	0.49	0.74	33	empty
2	53	0.25	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 300 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

1J83 · Structure of FAM17 carbohydrate binding module from clostridium cellulovorans · 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 P94622
Elsewhere: RCSB PDB 1J83 · PDBe 1J83 · UniProt P94622

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