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Designed protein KE59 R13 3/11H

Analyse Designed protein KE59 R13 3/11H in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3UZ5
Type: protein
Length: 494 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kemp eliminase KE59 R13 3/11H
EC: 4.-.-.-
Ligands: 0CU, NA, PO4
Pockets: 3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Kemp eliminase KE59 R13 3/11H (EC 4.-.-.-)	protein	247	42% helix, 17% strand	—

Ligands and binding sites

0CU · 5,7-dichloro-1H-benzotriazole · ligand · 2 copies · chains A, B
NA · Sodium ion · metal · 2 copies · chains A, B
PO4 · Phosphate ion · ion · 4 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	233	0.78	0.91	43	0CU, PO4
2	216	0.75	0.89	43	0CU, PO4
3	292	0.59	0.78	36	empty

Interfaces

1 interface between chains.

A–B · 216 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

3UZ5 · Designed protein KE59 R13 3/11H · the same entry in another collection · chain B against B, 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
Elsewhere: RCSB PDB 3UZ5 · PDBe 3UZ5

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