MolNFT v1 · #119110 · protein

Double-heterohexameric rings of full-length RVB1(ADP)RVB2(ADP)

5FM7: “Double-heterohexameric rings of full-length RVB1(ADP)RVB2(ADP)”. X-ray diffraction, 1 ligand (ADP), 13 pockets (best druggability 0.84). MolNFT v1 #119110 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5FM7
Type: protein
Length: 840 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RVB1; RVB2
UniProt: G0RYI5, G0RYC2
Ligands: ADP
Pockets: 13 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RVB1	protein	418	39% helix, 20% strand	G0RYI5
B	RVB2	protein	422	36% helix, 23% strand	G0RYC2

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B

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

Pockets

13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	953	0.84	0.86	101	ADP
2	542	0.67	0.78	57	empty
3	274	0.66	0.82	37	ADP
4	191	0.59	0.82	27	empty
5	105	0.56	0.84	25	empty

Interfaces

1 interface between chains.

A–B · 2493 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

5FM7 · Double-heterohexameric rings of full-length Rvb1(ADP)Rvb2(ADP) · 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 G0RYI5
Every structure of UniProt G0RYC2
Elsewhere: RCSB PDB 5FM7 · PDBe 5FM7 · UniProt G0RYI5 · UniProt G0RYC2

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