Research workbench

V. cholera biofilm scaffolding protein rbma

Analyse V. cholera biofilm scaffolding protein rbma in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BE6
Type: protein
Length: 459 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rbma
UniProt: C3NSJ9
Ligands: K, CA
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 63% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rbma	protein	225	0% helix, 64% strand	C3NSJ9
B	Rbma	protein	234	1% helix, 61% strand	C3NSJ9

Ligands and binding sites

K · Potassium ion · metal · chains A, B
CA · Calcium ion · metal · chains B
GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1117	0.78	0.80	117	K
2	153	0.54	0.80	28	GOL
3	74	0.32	0.74	21	GOL

Interfaces

1 interface between chains.

A–B · 2440 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

4BE6 · V. cholera biofilm scaffolding protein RbmA · 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 C3NSJ9
Elsewhere: RCSB PDB 4BE6 · PDBe 4BE6 · UniProt C3NSJ9

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