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Procarboxypeptidase ternary complex

Analyse Procarboxypeptidase ternary complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1KBC
Type: protein
Length: 332 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Neutrophil collagenase
EC: 3.4.24.34
UniProt: P22894
Ligands: CA, ZN

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Neutrophil collagenase (EC 3.4.24.34)	protein	166	24% helix, 17% strand	P22894

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A, B
ZN · Zinc ion · metal · 4 copies · chains A, B

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

Interfaces

1 interface between chains.

A–B · 127 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 4 modified (nonstandard).

Compared structures

1KBC · Procarboxypeptidase ternary complex · the same entry in another collection · chain A against A, TM-score 1.00
P22894 · AlphaFold monomer V2.0 prediction for neutrophil collagenase (P22894) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P22894
Elsewhere: RCSB PDB 1KBC · PDBe 1KBC · UniProt P22894

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