Structure of PDB 5uwn Chain B

Receptor sequence
>5uwnB (length=170) Species: 9606 (Homo sapiens) [Search protein sequence]
YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYGPGDEDP
3D structure
PDB5uwn Structure-Based Design and Synthesis of Potent and Selective Matrix Metalloproteinase 13 Inhibitors.
ChainB
Resolution3.2 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 H222 H226 H232 H119 H123 H129
BS02 ZN B H172 D174 H187 H200 H69 D71 H84 H97
BS03 CA B D179 G180 S182 L184 D202 E205 D76 G77 S79 L81 D99 E102
BS04 CA B D162 N194 G196 D198 D59 N91 G93 D95
BS05 8O7 B L184 L185 A186 L218 H222 L239 F241 P242 I243 Y244 T245 T247 L81 L82 A83 L115 H119 L136 F138 P139 I140 Y141 T142 T144 BindingDB: Ki=14nM,IC50=8.3nM
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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Biological Process
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Cellular Component
External links
PDB RCSB:5uwn, PDBe:5uwn, PDBj:5uwn
PDBsum5uwn
PubMed28653849
UniProtP45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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