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Esterase CRME10 mutant-D178A

Analyse Esterase CRME10 mutant-D178A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7C29
Type: protein
Length: 378 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carboxylesterase
UniProt: A0A1Z1F9L9
Ligands: CA
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 52% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxylesterase	protein	190	53% helix, 14% strand	A0A1Z1F9L9
B	Carboxylesterase	protein	188	52% helix, 14% strand	A0A1Z1F9L9

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A, B
EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
ACT · Acetate ion · additive · 2 copies · chains B

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

Pockets

2 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	1106	0.72	0.76	83	empty
2	471	0.60	0.74	35	EDO

Interfaces

1 interface between chains.

A–B · 314 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

7C29 · Esterase CrmE10 mutant-D178A · 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 A0A1Z1F9L9
Elsewhere: RCSB PDB 7C29 · PDBe 7C29 · UniProt A0A1Z1F9L9

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