Structure of PDB 1ztq Chain C

Receptor sequence

>1ztqC (length=153) Species: 9606 (Homo sapiens)

YNVFLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRL
HDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDET
WTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTPDDDVQGIQSL
YGP

3D structure

• PDB: 1ztq Identification of potent and selective MMP-13 inhibitors
• Chain: C
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H197 E198 H201 H207
• Catalytic site (residue number reindexed from 1): H116 E117 H120 H126
• 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	H197 H201 H207	H116 H120 H126
BS02	ZN	C	H147 D149 H162 H175	H66 D68 H81 H94
BS03	CA	C	D154 G155 S157 L159 D177 E180	D73 G74 S76 L78 D96 E99
BS04	CA	C	D137 N169 G171 D173	D56 N88 G90 D92
BS05	CA	C	D103 D178 E180	D22 D97 E99
BS06	033	C	L159 L160 A161 L193 H197 E198 H207 G212 L214 F216 P217 I218 Y219 P230	L78 L79 A80 L112 H116 E117 H126 G131 L133 F135 P136 I137 Y138 P140	MOAD: ic50=1.3nM BindingDB: IC50=1.3nM

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

External links

• PDB: RCSB:1ztq, PDBe:1ztq, PDBj:1ztq
• PDBsum: 1ztq
• PubMed: 16005220
• UniProt: P45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)