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MolNFT v2 · #157027 · protein

Structural basis for broad specificity in alpha-lytic protease mutants

6LPR: “Structural basis for broad specificity in alpha-lytic protease mutants”. X-ray diffraction at 2.1, 1 ligand (SO4). MolNFT v2 #157027 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
6LPR
Type
protein
Length
202 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.1
Source
Lysobacter enzymogenes; SYNTHETIC CONSTRUCT
Molecule
Alpha-lytic protease; Methoxysuccinyl-ala-ala-pro-norleucine boronic acid inhibitor
EC
3.4.21.12
UniProt
P00778
Ligands
SO4

Structure

x-ray diffraction · resolution 2.1 · 2 distinct chains · 6% helix, 54% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-lytic protease (EC 3.4.21.12)protein1987% helix, 55% strandP00778
PMethoxysuccinyl-ala-ala-pro-norleucine boronic acid inhibitorprotein40% helix, 25% strand—

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A

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

Interfaces

1 interface between chains.

  • A–P · 370 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide, 1 modified (disulfide, nonstandard).

Compared structures

  • 6LPR · Structural basis for broad specificity in alpha-lytic protease mutants · the same entry in another collection · chain A against A, TM-score 1.00
  • P00778 · AlphaFold monomer V2.0 prediction for alpha-lytic protease (P00778) · a predicted model of the same protein · chain A against A, TM-score 1.00

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