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Crystal structure of the lipoprotein BT2263 from bacteroides thetaiotaomicron

Analyse Crystal structure of the lipoprotein BT2263 from bacteroides thetaiotaomicron in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FQ4
Type: protein
Length: 921 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative lipoprotein
UniProt: Q8A5H6
Ligands: CA
Pockets: 10 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 55% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative lipoprotein	protein	458	55% helix, 5% strand	Q8A5H6
B	Putative lipoprotein	protein	463	54% helix, 5% strand	Q8A5H6

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

10 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	1157	0.83	0.84	109	empty
2	229	0.49	0.74	46	empty
3	142	0.47	0.77	19	empty
4	126	0.41	0.75	37	empty
5	81	0.36	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 656 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5FQ4 · Crystal structure of the lipoprotein BT2263 from Bacteroides thetaiotaomicron · 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 Q8A5H6
Elsewhere: RCSB PDB 5FQ4 · PDBe 5FQ4 · UniProt Q8A5H6

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