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1.65 a structure of cleaved viral serpin crma

Analyse 1.65 a structure of cleaved viral serpin crma in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1M93
Type
protein
Length
322 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Serine proteinase inhibitor 2
UniProt
P07385
Ligands
PO4
Pockets
2 · best druggability 0.45

Structure

x-ray diffraction · 3 distinct chains · 23% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASerine proteinase inhibitor 2protein4667% helix, 7% strandP07385
BSerine proteinase inhibitor 2protein24518% helix, 43% strandP07385
CSerine proteinase inhibitor 2protein310% helix, 55% strandP07385

Ligands and binding sites

  • PO4 · Phosphate ion · ion · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11440.450.7625empty
2920.410.7819empty

Interfaces

3 interfaces between chains.

  • A–B · 1800 Ų buried · 24 hydrogen bonds · protein-protein
  • B–C · 1755 Ų buried · 22 hydrogen bonds · protein-protein
  • A–C · 588 Ų buried · 17 hydrogen bonds · protein-protein

Compared structures

  • 1M93 · 1.65 A Structure of Cleaved Viral Serpin CRMA · the same entry in another collection · chain B against B, TM-score 1.00

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