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Directed evolutionary changes in kemp eliminase KE07 - crystal 11 round 6

Analyse Directed evolutionary changes in kemp eliminase KE07 - crystal 11 round 6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5D32
Type: protein
Length: 510 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: De novo kemp eliminase KE07 round 6
EC: 4.1.3.-
Pockets: 5 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	De novo kemp eliminase KE07 round 6 (EC 4.1.3.-)	protein	249	40% helix, 24% strand	—
B	De novo kemp eliminase KE07 round 6 (EC 4.1.3.-)	protein	261	38% helix, 23% strand	—

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	359	0.64	0.79	45	empty
2	232	0.61	0.80	25	empty
3	213	0.49	0.75	27	empty
4	52	0.46	0.85	16	empty
5	132	0.40	0.75	29	empty

Interfaces

1 interface between chains.

A–B · 463 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

5D32 · Directed evolutionary changes in Kemp Eliminase KE07 - Crystal 11 round 6 · 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
Elsewhere: RCSB PDB 5D32 · PDBe 5D32

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