MolNFT v1 · #161210 · protein

The structure of GH26A from muricauda sp. MAR_2010_75

6Q75: “The structure of GH26A from muricauda sp. MAR_2010_75”. X-ray diffraction, 4 pockets (best druggability 0.70). MolNFT v1 #161210 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6Q75
Type: protein
Length: 616 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GH26A
Pockets: 4 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GH26A	protein	310	40% helix, 17% strand	—
B	GH26A	protein	306	40% helix, 18% strand	—

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

4 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	760	0.70	0.76	90	TRS, GOL
2	66	0.35	0.77	17	empty
3	104	0.34	0.73	19	empty
4	55	0.31	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 636 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

6Q75 · The structure of GH26A from Muricauda sp. MAR_2010_75 · 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
Elsewhere: RCSB PDB 6Q75 · PDBe 6Q75

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