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Structure of apo bipa

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

PDB: 5A9V
Type: protein
Length: 3,330 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTP-binding protein
UniProt: B7MHF0
Pockets: 20 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	GTP-binding protein	protein	555	20% helix, 28% strand	B7MHF0

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	762	0.76	0.80	99	empty
2	731	0.74	0.80	84	empty
3	674	0.73	0.80	78	empty
4	670	0.73	0.80	83	empty
5	793	0.71	0.77	74	empty

Interfaces

5 interfaces between chains.

E–F · 1704 Å² buried · 12 hydrogen bonds · protein-protein
B–C · 1703 Å² buried · 13 hydrogen bonds · protein-protein
D–F · 899 Å² buried · 8 hydrogen bonds · protein-protein
A–E · 893 Å² buried · 8 hydrogen bonds · protein-protein
C–D · 280 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

5A9V · Structure of apo BipA · the same entry in another collection · chain D against D, 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 B7MHF0
Elsewhere: RCSB PDB 5A9V · PDBe 5A9V · UniProt B7MHF0

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