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Crystal structure of oxag

Analyse Crystal structure of oxag in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5W7K
Type: protein
Length: 543 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oxag
UniProt: A0A1B2TT18
Ligands: SAH, CL
Pockets: 4 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oxag	protein	274	48% helix, 26% strand	A0A1B2TT18
B	Oxag	protein	269	45% helix, 26% strand	A0A1B2TT18

Ligands and binding sites

SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
CL · Chloride ion · ion · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	661	0.74	0.80	54	SAH
2	654	0.74	0.80	51	SAH
3	527	0.69	0.79	43	empty
4	166	0.53	0.80	26	empty

Interfaces

1 interface between chains.

A–B · 492 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

5W7K · Crystal structure of OxaG · the same entry in another collection · chain B against B, 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 A0A1B2TT18
Elsewhere: RCSB PDB 5W7K · PDBe 5W7K · UniProt A0A1B2TT18

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