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Human plasminogen activator inhibitor-2.[LOOP (66-98) deletion mutant] complexed with peptide N-acetyl-teaaagdggvmtgr-oh

Analyse Human plasminogen activator inhibitor-2.[LOOP (66-98) deletion mutant]… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2ARQ
Type
protein
Length
374 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Plasminogen activator inhibitor-2; 14-mer from plasminogen activator inhibitor-2
UniProt
P05120
Ligands
ACE
Pockets
1 · best druggability 0.34

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APlasminogen activator inhibitor-2protein36031% helix, 34% strandP05120
P14-mer from plasminogen activator inhibitor-2protein140% helix, 86% strandP05120

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains A, P

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1560.340.7814empty

Interfaces

1 interface between chains.

  • A–P · 1343 Ų buried · 50 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).

Compared structures

  • 2ARQ · Human plasminogen activator inhibitor-2.[loop (66-98) deletion mutant] complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
  • P05120 · AlphaFold monomer V2.0 prediction for plasminogen activator inhibitor 2 (P05120) · a predicted model of the same protein · chain A against A, TM-score 0.94

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