Structure of PDB 1ztq Chain A

Receptor sequence
>1ztqA (length=162) Species: 9606 (Homo sapiens) [Search protein sequence]
YNVFLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRL
HDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDET
WTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPD
DDVQGIQSLYGP
3D structure
PDB1ztq Identification of potent and selective MMP-13 inhibitors
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 A H197 H201 H207 H116 H120 H126
BS02 ZN A H147 D149 H162 H175 H66 D68 H81 H94
BS03 CA A D154 G155 S157 L159 D177 E180 D73 G74 S76 L78 D96 E99
BS04 CA A D137 N169 G171 D173 D56 N88 G90 D92
BS05 CA A D103 D178 E180 D22 D97 E99
BS06 033 A L159 L160 A161 H197 E198 H201 H207 G212 L214 F216 P217 I218 Y219 T220 F227 P230 L78 L79 A80 H116 E117 H120 H126 G131 L133 F135 P136 I137 Y138 T139 F146 P149 MOAD: ic50=1.3nM
PDBbind-CN: -logKd/Ki=8.89,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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ztq, PDBe:1ztq, PDBj:1ztq
PDBsum1ztq
PubMed16005220
UniProtP45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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