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Catalytic domain of human stromelysin-1 at pH 5.5 and 40OC complexed with inhibitor

Analyse Catalytic domain of human stromelysin-1 at pH 5.5 and 40OC complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2SRT
Type: protein
Length: 173 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Stromelysin-1
EC: 3.4.24.17
UniProt: P08254
Ligands: 8MI, ZN
Pockets: 1 · best druggability 0.44

Structure

solution nmr · 1 distinct chain · 24% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Stromelysin-1 (EC 3.4.24.17)	protein	173	24% helix, 10% strand	P08254

Ligands and binding sites

8MI · N-(R-carboxy-ethyl)-alpha-(S)-(2-phenylethyl)glycyl-L-arginine-N-phenylamide · ligand · chains A
ZN · Zinc 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	110	0.44	0.78	20	8MI

Compared structures

2SRT · Catalytic domain of human stromelysin-1 at pH 5.5 and 40OC complexed with inhibitor · the same entry in another collection · 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 P08254
Elsewhere: RCSB PDB 2SRT · PDBe 2SRT · UniProt P08254

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