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Cmcb E35G mutant from type II cut mcp

Analyse Cmcb E35G mutant from type II cut mcp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MN4
Type: protein
Length: 541 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bmc domain-containing protein
UniProt: Q8G9V6
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, E, F	Bmc domain-containing protein	protein	90	43% helix, 34% strand	Q8G9V6
D	Bmc domain-containing protein	protein	91	43% helix, 34% strand	Q8G9V6

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	144	0.36	0.72	24	empty

Interfaces

6 interfaces between chains.

D–E · 981 Å² buried · 9 hydrogen bonds · protein-protein
C–D · 945 Å² buried · 9 hydrogen bonds · protein-protein
A–B · 942 Å² buried · 9 hydrogen bonds · protein-protein
E–F · 938 Å² buried · 9 hydrogen bonds · protein-protein
B–C · 927 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

7MN4 · CmcB E35G mutant from Type II Cut MCP · 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 Q8G9V6
Elsewhere: RCSB PDB 7MN4 · PDBe 7MN4 · UniProt Q8G9V6

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