Research workbench

CAS6-rt-CAS1--CAS2 complex

Analyse CAS6-rt-CAS1--CAS2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7KFU
Type: protein
Length: 2,674 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CAS2; CAS6-rt-CAS1
Pockets: 20 · best druggability 0.79

Structure

electron microscopy · 3 distinct chains · 42% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	CAS2	protein	96	31% helix, 27% strand	—
C, E	CAS6-rt-CAS1	protein	909	41% helix, 16% strand	—
D, F	CAS6-rt-CAS1	protein	332	47% helix, 16% strand	—

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	308	0.79	0.89	52	empty
2	294	0.77	0.88	54	empty
3	794	0.71	0.77	81	empty
4	700	0.70	0.77	76	empty
5	511	0.69	0.79	48	empty

Interfaces

9 interfaces between chains.

C–F · 1707 Å² buried · 10 hydrogen bonds · protein-protein
D–E · 1665 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 1572 Å² buried · 24 hydrogen bonds · protein-protein
B–E · 1350 Å² buried · 15 hydrogen bonds · protein-protein
A–C · 1285 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

7KFU · Cas6-RT-Cas1--Cas2 complex · 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
Elsewhere: RCSB PDB 7KFU · PDBe 7KFU

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