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Saxiphilin apo structure

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

PDB: 6O0D
Type: protein
Length: 1,627 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Saxiphilin
UniProt: P31226
Pockets: 20 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Saxiphilin	protein	810	27% helix, 17% strand	P31226
B	Saxiphilin	protein	817	26% helix, 18% strand	P31226

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1039	0.78	0.80	106	empty
2	1127	0.76	0.78	108	empty
3	1127	0.72	0.76	101	empty
4	148	0.68	0.89	30	empty
5	170	0.68	0.88	34	empty

Interfaces

1 interface between chains.

A–B · 309 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 42 disulfide (disulfide).

Compared structures

6O0D · Saxiphilin Apo structure · the same entry in another collection · chain A against A, TM-score 1.00
P31226 · AlphaFold monomer V2.0 prediction for saxiphilin (P31226) · a predicted model of the same protein · chain B against A, TM-score 0.76

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 P31226
Elsewhere: RCSB PDB 6O0D · PDBe 6O0D · UniProt P31226

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