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Crystal structure of carboxyl-terminal processing protease a mutant S302A, CTPA_S302A, of pseudomonas aeruginosa

Analyse Crystal structure of carboxyl-terminal processing protease a mutant S302A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7RQH
Type
protein
Length
516 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Probable carboxyl-terminal protease
UniProt
Q9HU50
Pockets
1 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProbable carboxyl-terminal proteaseprotein25835% helix, 24% strandQ9HU50
BProbable carboxyl-terminal proteaseprotein25834% helix, 24% strandQ9HU50

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12010.750.9135empty

Interfaces

1 interface between chains.

  • A–B · 774 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 7RQH · Crystal Structure of carboxyl-terminal processing protease A mutant S302A, CtpA_S302A, of… · the same entry in another collection · chain A against A, TM-score 1.00

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