Structure of PDB 830c Chain A

Receptor sequence
>830cA (length=164) Species: 9606 (Homo sapiens) [Search protein sequence]
YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTFMLPDD
DVQGIQSLYGPGDE
3D structure
PDB830c Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors.
ChainA
Resolution1.6 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 A H222 H226 H232 H119 H123 H129
BS02 ZN A H172 D174 H187 H200 H69 D71 H84 H97
BS03 CA A D179 G180 S182 L184 D202 E205 D76 G77 S79 L81 D99 E102
BS04 RS1 A L185 A186 H222 E223 H226 H232 L239 F241 I243 Y244 L82 A83 H119 E120 H123 H129 L136 F138 I140 Y141 MOAD: Ki=0.52nM
PDBbind-CN: -logKd/Ki=9.28,Ki=0.52nM
BindingDB: IC50=0.010000nM,Ki=0.52nM
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:830c, PDBe:830c, PDBj:830c
PDBsum830c
PubMed10074939
UniProtP45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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