MolNFT v1 · #86690 · protein

V. cholera biofilm scaffolding protein rbma

4BE5: “V. cholera biofilm scaffolding protein rbma”. X-ray diffraction, 1 ligand (NA), 3 pockets (best druggability 0.78). MolNFT v1 #86690 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4BE5
Type: protein
Length: 458 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rbma
UniProt: C3NSJ9
Ligands: NA
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	224	1% helix, 65% strand	C3NSJ9
B	Rbma	protein	234	1% helix, 61% strand	C3NSJ9

Ligands and binding sites

NA · Sodium ion · metal · chains A
GOL · Glycerol · additive · 2 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	1132	0.78	0.80	109	empty
2	109	0.52	0.82	19	empty
3	54	0.28	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 2511 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

4BE5 · 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 4BE5 · PDBe 4BE5 · UniProt C3NSJ9

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