Structure of PDB 4l19 Chain B

Receptor sequence
>4l19B (length=170) Species: 9606 (Homo sapiens) [Search protein sequence]
YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYGPGDEDP
3D structure
PDB4l19 Characterization of selective exosite-binding inhibitors of matrix metalloproteinase 13 that prevent articular cartilage degradation in vitro.
ChainB
Resolution1.66 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 B H172 D174 H187 H200 H69 D71 H84 H97
BS02 ZN B H222 H226 H232 H119 H123 H129
BS03 CA B D162 N194 G196 D198 D59 N91 G93 D95
BS04 CA B D179 G180 S182 L184 D202 E205 D76 G77 S79 L81 D99 E102
BS05 1UA B H222 L239 F241 I243 Y244 T245 P255 H119 L136 F138 I140 Y141 T142 P152 MOAD: Ki=0.8uM
BindingDB: IC50=2400nM,Ki=824nM
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:4l19, PDBe:4l19, PDBj:4l19
PDBsum4l19
PubMed25330343
UniProtP45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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