Structure of PDB 5uwn Chain E

Receptor sequence

>5uwnE (length=167) Species: 9606 (Homo sapiens) [Search protein sequence]

MYNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLN
FTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFD
DDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHF
MLPDDDVQGIQSLYGPG

3D structure

PDB

5uwn Structure-Based Design and Synthesis of Potent and Selective Matrix Metalloproteinase 13 Inhibitors.

Chain

Resolution

3.2 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Catalytic site (original residue number in PDB)	H222 E223 H226 H232
Catalytic site (residue number reindexed from 1)	H120 E121 H124 H130
Enzyme Commision number	3.4.24.-

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	E	H222 H226 H232	H120 H124 H130
BS02	ZN	E	H172 D174 H187 H200	H70 D72 H85 H98
BS03	CA	E	D179 G180 P181 S182 L184 D202 E205	D77 G78 P79 S80 L82 D100 E103
BS04	CA	E	D162 N194 G196 D198	D60 N92 G94 D96
BS05	8O7	E	M103 Y104 L184 L185 A186 H222 E223 A238 L239 F241 P242 I243 Y244 T245 T247 P255	M1 Y2 L82 L83 A84 H120 E121 A136 L137 F139 P140 I141 Y142 T143 T145 P153	BindingDB: Ki=14nM,IC50=8.3nM

Gene Ontology

	Molecular Function
GO:0004222	metalloendopeptidase activity
GO:0008237	metallopeptidase activity
GO:0008270	zinc ion binding

	Biological Process
GO:0006508	proteolysis

	Cellular Component
GO:0031012	extracellular matrix

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:5uwn, PDBe:5uwn, PDBj:5uwn
PDBsum	5uwn
PubMed	28653849
UniProt	P45452\|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

[Back to BioLiP]