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Tailoring enzyme stability and exploiting stability-trait linkage by iterative truncation and optimization

Analyse Tailoring enzyme stability and exploiting stability-trait linkage by iterative… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TOI
Type: protein
Length: 493 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ampicillin resistance protein
EC: 3.5.2.6
UniProt: Q79DR3
Pockets: 3 · best druggability 0.34

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ampicillin resistance protein (EC 3.5.2.6)	protein	248	41% helix, 19% strand	Q79DR3
B	Ampicillin resistance protein (EC 3.5.2.6)	protein	245	42% helix, 20% strand	Q79DR3

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	98	0.34	0.74	18	empty
2	71	0.33	0.75	18	empty
3	72	0.31	0.75	15	empty

Interfaces

1 interface between chains.

A–B · 484 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3TOI · Tailoring Enzyme Stability and Exploiting Stability-Trait Linkage by Iterative Truncation… · 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 Q79DR3
Elsewhere: RCSB PDB 3TOI · PDBe 3TOI · UniProt Q79DR3

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