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Crystal structure of the K. lactis urea amidolyase

Analyse Crystal structure of the K. lactis urea amidolyase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5I8I
Type: protein
Length: 6,636 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Urea amidolyase
UniProt: Q6CP22
Pockets: 20 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Urea amidolyase	protein	1660	29% helix, 26% strand	Q6CP22
B, D	Urea amidolyase	protein	1658	29% helix, 26% strand	Q6CP22

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	595	0.81	0.86	89	empty
2	291	0.79	0.91	55	empty
3	599	0.76	0.83	71	empty
4	574	0.76	0.83	69	empty
5	578	0.76	0.82	68	empty

Interfaces

3 interfaces between chains.

C–D · 3780 Å² buried · 76 hydrogen bonds · protein-protein
A–B · 3721 Å² buried · 63 hydrogen bonds · protein-protein
A–D · 615 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

5I8I · Crystal Structure of the K. lactis Urea Amidolyase · 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 5I8I · PDBe 5I8I · UniProt Q6CP22

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