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Subtilisin bpn' 8397+1 (E.C. 3.4.21.14) (mutant with met 50 replaced by phe, asn 76 replaced by asp, gly 169 replaced by ala, gln 206 replaced by cys, asn 218 replaced by ser and lys 256 replaced by tyr) (M50F, N76D, G169A, Q206C, N218S, and K256Y) in 35% dimethylformamide

Analyse Subtilisin bpn' 8397+1 (E.C. 3.4.21.14) (mutant with met 50 replaced by phe… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1YJB
Type
protein
Length
275 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Subtilisin 8397+1
EC
3.4.21.14
UniProt
P00782
Ligands
CA
Pockets
1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASubtilisin 8397+1 (EC 3.4.21.14)protein27531% helix, 20% strandP00782

Ligands and binding sites

  • CA · Calcium ion · metal · 2 copies · chains A

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
1970.360.7523empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

  • 1YJB · Subtilisin bpn' 8397+1 (E.C. 3.4.21.14) (mutant with met 50 replaced by phe, asn 76… · the same entry in another collection · chain A against A, TM-score 1.00

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