Structure of PDB 3kry Chain C

Receptor sequence

>3kryC (length=164) Species: 9606 (Homo sapiens)

YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYG

3D structure

• PDB: 3kry Orally-active MMP-1 sparing alpha-tetrahydropyranyl and alpha-piperidinyl sulfone matrix metalloproteinase (MMP) inhibitors with efficacy in cancer, arthritis, and cardiovascular disease
• Chain: C
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H222 E223 H226 H232
• Catalytic site (residue number reindexed from 1): H119 E120 H123 H129
• 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	C	H172 D174 H187 H200	H69 D71 H84 H97
BS02	ZN	C	H222 H226 H232	H119 H123 H129
BS03	CA	C	D162 N194 G196 D198	D59 N91 G93 D95
BS04	CA	C	D179 G180 S182 L184 D202 E205	D76 G77 S79 L81 D99 E102
BS05	3KR	C	L184 L185 A186 L218 H222 E223 H226 H232 L239 F241 P242 I243 Y244 T245	L81 L82 A83 L115 H119 E120 H123 H129 L136 F138 P139 I140 Y141 T142	MOAD: ic50=0.1nM

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

External links

• PDB: RCSB:3kry, PDBe:3kry, PDBj:3kry
• PDBsum: 3kry
• PubMed: 20726512
• UniProt: P45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)