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Crystal structure of clostridium histolyticum colg collagenase pkd domain 2 at 1.6 ångström resolution

Analyse Crystal structure of clostridium histolyticum colg collagenase pkd domain 2 at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4JRW
Type: protein
Length: 174 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Collagenase
UniProt: Q9X721
Ligands: BR
Pockets: 2 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Collagenase	protein	87	0% helix, 57% strand	Q9X721

Ligands and binding sites

BR · Bromide ion · ion · chains B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	59	0.36	0.79	12	empty
2	62	0.31	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 684 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

4JRW · Crystal structure of Clostridium histolyticum colg collagenase PKD domain 2 at 1.6… · the same entry in another collection · chain A against A, TM-score 1.00
Q9X721 · AlphaFold monomer V2.0 prediction for collagenase colg (Q9X721) · a predicted model of the same protein · chain B against A, TM-score 0.96

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 Q9X721
Elsewhere: RCSB PDB 4JRW · PDBe 4JRW · UniProt Q9X721

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