MolNFT v1 · #123922 · protein

Structure of wild type amidase from vibrio cholerae 0395 at low temparature at 1.8 ångströms resolution.

5JZM · Intracellular PROTEASE/AMIDASE: “Structure of wild type amidase from vibrio cholerae 0395 at low temparature at 1.8 ångströms resolution.”. X-ray diffraction, 15 pockets (best druggability 0.76). MolNFT v1 #123922 on GenesisL1: 3D…

PDB: 5JZM
Type: protein
Length: 1,686 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Intracellular PROTEASE/AMIDASE
EC: 4.2.1.130
UniProt: A0A0H3AFW5
Pockets: 15 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Intracellular PROTEASE/AMIDASE (EC 4.2.1.130)	protein	281	37% helix, 17% strand	A0A0H3AFW5

Pockets

15 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	558	0.76	0.83	63	empty
2	644	0.72	0.79	71	empty
3	173	0.68	0.87	36	empty
4	185	0.67	0.86	45	empty
5	360	0.61	0.78	52	empty

Interfaces

10 interfaces between chains.

C–D · 1086 Å² buried · 21 hydrogen bonds · protein-protein
A–B · 1084 Å² buried · 19 hydrogen bonds · protein-protein
E–F · 913 Å² buried · 16 hydrogen bonds · protein-protein
C–F · 470 Å² buried · 10 hydrogen bonds · protein-protein
B–F · 384 Å² buried · 4 hydrogen bonds · protein-protein

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 A0A0H3AFW5
Elsewhere: RCSB PDB 5JZM · PDBe 5JZM · UniProt A0A0H3AFW5

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