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The structure of carboxypeptidase from fusobacterium nucleatum

Analyse The structure of carboxypeptidase from fusobacterium nucleatum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EP9
Type: protein
Length: 2,640 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: S9 family peptidase
UniProt: A0A1S1MBE1
Pockets: 20 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
G, A, B, C	S9 family peptidase	protein	660	21% helix, 39% strand	A0A1S1MBE1

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	778	0.73	0.78	84	empty
2	1111	0.72	0.76	83	empty
3	497	0.71	0.81	74	empty
4	426	0.69	0.81	59	empty
5	707	0.68	0.76	56	empty

Interfaces

4 interfaces between chains.

G–A · 2601 Å² buried · 40 hydrogen bonds · protein-protein
B–C · 2581 Å² buried · 40 hydrogen bonds · protein-protein
A–C · 685 Å² buried · 11 hydrogen bonds · protein-protein
G–B · 658 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

7EP9 · The structure of carboxypeptidase from Fusobacterium nucleatum · the same entry in another collection · chain G against G, 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 A0A1S1MBE1
Elsewhere: RCSB PDB 7EP9 · PDBe 7EP9 · UniProt A0A1S1MBE1

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