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Hyperthermophilic esterase from the archeon pyrobaculum calidifontis

Analyse Hyperthermophilic esterase from the archeon pyrobaculum calidifontis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZWQ
Type: protein
Length: 618 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ALPHA/BETA hydrolase fold-3 domain protein
EC: 3.1.1.1
UniProt: A3MVR4
Pockets: 4 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ALPHA/BETA hydrolase fold-3 domain protein (EC 3.1.1.1)	protein	313	43% helix, 21% strand	A3MVR4
B	ALPHA/BETA hydrolase fold-3 domain protein (EC 3.1.1.1)	protein	305	43% helix, 21% strand	A3MVR4

Pockets

4 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	581	0.83	0.88	63	empty
2	542	0.75	0.82	64	empty
3	88	0.44	0.80	13	empty
4	61	0.33	0.76	10	empty

Interfaces

1 interface between chains.

A–B · 1401 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

3ZWQ · Hyperthermophilic esterase from the archeon pyrobaculum calidifontis · 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 A3MVR4
Elsewhere: RCSB PDB 3ZWQ · PDBe 3ZWQ · UniProt A3MVR4

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