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Crystal structure of G56E-PROPEPTIDE:S324A-subtilisin complex

Analyse Crystal structure of G56E-PROPEPTIDE:S324A-subtilisin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Z57
Type: protein
Length: 383 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tk-subtilisin
EC: 3.4.21.62
UniProt: P58502
Ligands: CA, ZN

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tk-subtilisin (EC 3.4.21.62)	protein	318	29% helix, 20% strand	P58502
B	Tk-subtilisin (EC 3.4.21.62)	protein	65	25% helix, 38% strand	P58502

Ligands and binding sites

CA · Calcium ion · metal · 7 copies · chains A
ZN · Zinc ion · metal · chains B

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

Interfaces

1 interface between chains.

A–B · 1253 Å² buried · 28 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2Z57 · Crystal structure of G56E-propeptide:S324A-subtilisin complex · the same entry in another collection · chain A against A, TM-score 1.00
P58502 · AlphaFold monomer V2.0 prediction for tk-subtilisin (P58502) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P58502
Elsewhere: RCSB PDB 2Z57 · PDBe 2Z57 · UniProt P58502

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