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1.93 Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria gonorrhoeae.

Analyse 1.93 Angstrom Resolution Crystal Structure of Peptidase M23 from Neisseria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MUK
Type: protein
Length: 363 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.93
Source: Neisseria gonorrhoeae
Molecule: Peptidase M23
UniProt: Q5F676
Ligands: ZN
Pockets: 4 · best druggability 0.67

Structure

x-ray diffraction · resolution 1.93 · 1 distinct chain · 18% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidase M23	protein	363	18% helix, 40% strand	Q5F676

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	433	0.67	0.79	77	empty
2	98	0.51	0.83	26	empty
3	68	0.39	0.79	21	empty
4	66	0.33	0.77	16	empty

Compared structures

6MUK · 1.93 ångström resolution crystal structure of peptidase M23 from neisseria gonorrhoeae. · 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 Q5F676
Elsewhere: RCSB PDB 6MUK · PDBe 6MUK · UniProt Q5F676

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