MolNFT v1 · #30170 · protein

Structure of double mutant, D164N, E78H of kumamolisin-as

1ZVK: “Structure of double mutant, D164N, E78H of kumamolisin-as”. X-ray diffraction, 1 ligand (CA), 5 pockets (best druggability 0.60). MolNFT v1 #30170 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1ZVK
Type: protein
Length: 708 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kumamolisin-as
UniProt: Q8GB88
Ligands: CA
Pockets: 5 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Kumamolisin-as	protein	354	31% helix, 22% strand	Q8GB88

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	358	0.60	0.77	43	empty
2	60	0.41	0.81	16	empty
3	118	0.38	0.74	25	empty
4	96	0.34	0.74	20	empty
5	61	0.32	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 600 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

1ZVK · Structure of Double mutant, D164N, E78H of Kumamolisin-As · 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 Q8GB88
Elsewhere: RCSB PDB 1ZVK · PDBe 1ZVK · UniProt Q8GB88

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