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Cellulomonas fimi endo-beta-1,4-mannanase double mutant

Analyse Cellulomonas fimi endo-beta-1,4-mannanase double mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X2Y
Type: protein
Length: 901 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MAN26A
EC: 3.2.1.78
UniProt: Q9XCV5
Ligands: MG
Pockets: 6 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MAN26A (EC 3.2.1.78)	protein	450	28% helix, 24% strand	Q9XCV5
B	MAN26A (EC 3.2.1.78)	protein	451	29% helix, 23% strand	Q9XCV5

Ligands and binding sites

MG · Magnesium ion · metal · 4 copies · chains A, B
FMT · Formic acid · additive · 8 copies · chains A, B

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

Pockets

6 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	1196	0.74	0.77	124	FMT
2	123	0.45	0.78	23	empty
3	118	0.42	0.76	23	FMT
4	87	0.41	0.79	27	empty
5	67	0.38	0.79	23	empty

Interfaces

1 interface between chains.

A–B · 565 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

2X2Y · Cellulomonas fimi endo-beta-1,4-mannanase double mutant · 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 Q9XCV5
Elsewhere: RCSB PDB 2X2Y · PDBe 2X2Y · UniProt Q9XCV5

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