Structure of PDB 3kej Chain B

Receptor sequence

>3kejB (length=157) Species: 9606 (Homo sapiens)

TLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDG
IADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTS
SSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDV
QGIQSLY

3D structure

• PDB: 3kej Discovery of (pyridin-4-yl)-2H-tetrazole as a novel scaffold to identify highly selective matrix metalloproteinase-13 inhibitors for the treatment of osteoarthritis.
• Chain: B
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H222 E223 H226 H232
• Catalytic site (residue number reindexed from 1): H113 E114 H117 H123
• 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	B	H222 H226 H232	H113 H117 H123
BS02	ZN	B	H172 D174 H187 H200	H63 D65 H78 H91
BS03	CA	B	D179 G180 S182 L184 D202 E205	D70 G71 S73 L75 D93 E96
BS04	CA	B	D162 N194 G196 D198	D53 N85 G87 D89
BS05	CA	B	D128 E205 T206	D19 E96 T97
BS06	3EJ	B	K140 N215 F217 L218 H222 A238 L239 F241 I243 Y244 T245 T247 K249 F252	K31 N106 F108 L109 H113 A129 L130 F132 I134 Y135 T136 T138 K140 F143	MOAD: Ki=75.9nM BindingDB: Ki=76nM

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:3kej, PDBe:3kej, PDBj:3kej
• PDBsum: 3kej
• PubMed: 20005097
• UniProt: P45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)