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Crystal structure of the mutant M3+S202W/I203F of the esterase E40

Analyse Crystal structure of the mutant M3+S202W/I203F of the esterase E40 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GMR
Type: protein
Length: 1,188 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Esterase
UniProt: A0A0F6WGE1
Pockets: 9 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, A, B, D	Esterase	protein	297	44% helix, 18% strand	A0A0F6WGE1

Pockets

9 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	161	0.78	0.94	30	empty
2	181	0.76	0.92	33	empty
3	139	0.75	0.93	30	empty
4	156	0.74	0.91	28	empty
5	249	0.70	0.85	23	empty

Interfaces

4 interfaces between chains.

C–B · 726 Å² buried · 7 hydrogen bonds · protein-protein
C–A · 376 Å² buried · 7 hydrogen bonds · protein-protein
B–D · 372 Å² buried · 6 hydrogen bonds · protein-protein
A–D · 184 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

5GMR · Crystal structure of the mutant M3+S202W/I203F of the esterase E40 · the same entry in another collection · chain C against C, 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 A0A0F6WGE1
Elsewhere: RCSB PDB 5GMR · PDBe 5GMR · UniProt A0A0F6WGE1

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