MolNFT v1 · #50032 · protein

Crystal form B1

2R6D · Replicative helicase: “Crystal form B1”. X-ray diffraction, 20 pockets (best druggability 0.77). MolNFT v1 #50032 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2R6D
Type: protein
Length: 2,340 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Replicative helicase
UniProt: Q9X4C9
Pockets: 20 · best druggability 0.77

Structure

x-ray diffraction · 4 distinct chains · 50% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Replicative helicase	protein	405	52% helix, 14% strand	Q9X4C9
B, D	Replicative helicase	protein	376	49% helix, 15% strand	Q9X4C9
C	Replicative helicase	protein	399	50% helix, 13% strand	Q9X4C9
E, F	Replicative helicase	protein	392	48% helix, 14% strand	Q9X4C9

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	811	0.77	0.81	74	empty
2	748	0.76	0.81	73	empty
3	812	0.74	0.78	73	empty
4	861	0.71	0.76	75	empty
5	775	0.70	0.77	76	empty

Interfaces

9 interfaces between chains.

A–F · 2613 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 2503 Å² buried · 17 hydrogen bonds · protein-protein
D–E · 1929 Å² buried · 10 hydrogen bonds · protein-protein
E–F · 1597 Å² buried · 26 hydrogen bonds · protein-protein
A–B · 1575 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

2R6D · Crystal Form B1 · 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 Q9X4C9
Elsewhere: RCSB PDB 2R6D · PDBe 2R6D · UniProt Q9X4C9

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