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The crystal structure of ospa mutant

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

PDB: 3CKA
Type: protein
Length: 631 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Outer surface protein a
UniProt: D2Y4L7, Q45040
Pockets: 5 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Outer surface protein a	protein	315	3% helix, 57% strand	D2Y4L7, Q45040
B	Outer surface protein a	protein	316	4% helix, 56% strand	D2Y4L7, Q45040

Ligands and binding sites

1PE · Pentaethylene glycol · additive · 7 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1018	0.82	0.83	110	1PE
2	693	0.77	0.82	80	1PE
3	61	0.51	0.87	18	empty
4	115	0.40	0.75	20	1PE
5	117	0.39	0.75	24	1PE

Interfaces

1 interface between chains.

A–B · 1471 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

3CKA · The crystal structure of OspA 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 D2Y4L7
Every structure of UniProt Q45040
Elsewhere: RCSB PDB 3CKA · PDBe 3CKA · UniProt D2Y4L7 · UniProt Q45040

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