Structure of PDB 1ztq Chain B

Receptor sequence
>1ztqB (length=160) Species: 9606 (Homo sapiens) [Search protein sequence]
YNVKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHD
GIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWT
SSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDD
VQGIQSLYGP
3D structure
PDB1ztq Identification of potent and selective MMP-13 inhibitors
ChainB
Resolution2.0 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) H197 E198 H201 H207
Catalytic site (residue number reindexed from 1) H114 E115 H118 H124
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 H197 H201 H207 H114 H118 H124
BS02 ZN B H147 D149 H162 H175 H64 D66 H79 H92
BS03 CA B D154 G155 S157 L159 D177 E180 D71 G72 S74 L76 D94 E97
BS04 CA B D137 N169 G171 D173 D54 N86 G88 D90
BS05 CA B D103 D178 E180 D20 D95 E97
BS06 033 B L159 L160 A161 H197 E198 H207 L214 F216 P217 I218 Y219 T220 L76 L77 A78 H114 E115 H124 L131 F133 P134 I135 Y136 T137 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

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

[Back to BioLiP]