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Esterase domain of the ZFL2-1 ORF1 protein from the zebrafish ZFL2-1 retrotransposon

Analyse Esterase domain of the ZFL2-1 ORF1 protein from the zebrafish ZFL2-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4C1B
Type: protein
Length: 497 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ORF1-encoded protein
EC: 3.1.-.-
UniProt: Q3LG57
Pockets: 3 · best druggability 0.62

Structure

x-ray diffraction · 3 distinct chains · 48% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ORF1-encoded protein (EC 3.1.-.-)	protein	171	47% helix, 15% strand	Q3LG57
B	ORF1-encoded protein (EC 3.1.-.-)	protein	168	48% helix, 15% strand	Q3LG57
C	ORF1-encoded protein (EC 3.1.-.-)	protein	158	49% helix, 16% strand	Q3LG57

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	261	0.62	0.80	35	empty
2	99	0.43	0.78	19	empty
3	150	0.41	0.74	22	empty

Interfaces

2 interfaces between chains.

A–B · 3137 Å² buried · 42 hydrogen bonds · protein-protein
A–C · 463 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

4C1B · Esterase domain of the ZfL2-1 ORF1 protein from the zebrafish ZfL2-1 retrotransposon · 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 Q3LG57
Elsewhere: RCSB PDB 4C1B · PDBe 4C1B · UniProt Q3LG57

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