Research workbench

S177A kluyveromyces lactis allophanate hydrolase

Analyse S177A kluyveromyces lactis allophanate hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4IST
Type: protein
Length: 1,228 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Allophanate hydrolase
EC: 3.5.1.54
UniProt: Q6CP22
Pockets: 16 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Allophanate hydrolase (EC 3.5.1.54)	protein	614	34% helix, 19% strand	Q6CP22

Ligands and binding sites

TAR · D(-)-tartaric acid · additive · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	941	0.75	0.78	59	empty
2	338	0.67	0.81	39	TAR
3	325	0.66	0.81	41	TAR
4	140	0.52	0.80	27	empty
5	292	0.52	0.74	41	empty

Interfaces

1 interface between chains.

A–B · 2657 Å² buried · 26 hydrogen bonds · protein-protein

Compared structures

4IST · S177A Kluyveromyces lactis Allophanate Hydrolase · 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 Q6CP22
Elsewhere: RCSB PDB 4IST · PDBe 4IST · UniProt Q6CP22

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.