Structure of PDB 1xud Chain A

Receptor sequence
>1xudA (length=169) Species: 9606 (Homo sapiens) [Search protein sequence]
YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYGPGDED
3D structure
PDB1xud Structural basis for the highly selective inhibition of MMP-13.
ChainA
Resolution1.8 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 CA A D162 N194 Y195 G196 D198 D59 N91 Y92 G93 D95
BS05 PB4 A F217 L218 V219 H222 L239 F241 I243 Y244 T245 Y246 T247 S250 F252 F114 L115 V116 H119 L136 F138 I140 Y141 T142 Y143 T144 S147 F149 MOAD: ic50=8nM
PDBbind-CN: -logKd/Ki=8.10,IC50=8nM
BindingDB: IC50=8nM
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:1xud, PDBe:1xud, PDBj:1xud
PDBsum1xud
PubMed15734640
UniProtP45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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