MolNFT v1 · #122466 · protein

Crystal structure of esterase mutant - F72G

5IQ0: “Crystal structure of esterase mutant - F72G”. X-ray diffraction, 15 pockets (best druggability 0.78). MolNFT v1 #122466 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5IQ0
Type: protein
Length: 1,426 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
UniProt: Q4TZQ3
Pockets: 15 · best druggability 0.78

Structure

x-ray diffraction · 3 distinct chains · 40% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Esterase	protein	362	40% helix, 18% strand	Q4TZQ3
B, D	Esterase	protein	355	41% helix, 18% strand	Q4TZQ3
C	Esterase	protein	354	41% helix, 18% strand	Q4TZQ3

Pockets

15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	310	0.78	0.89	43	empty
2	293	0.78	0.89	43	empty
3	304	0.77	0.88	43	empty
4	263	0.75	0.88	40	empty
5	586	0.69	0.78	45	empty

Interfaces

3 interfaces between chains.

A–B · 1566 Å² buried · 24 hydrogen bonds · protein-protein
C–D · 1213 Å² buried · 18 hydrogen bonds · protein-protein
B–C · 375 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

5IQ0 · Crystal structure of Esterase mutant - F72G · 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 Q4TZQ3
Elsewhere: RCSB PDB 5IQ0 · PDBe 5IQ0 · UniProt Q4TZQ3

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