Structure of PDB 456c Chain A

Receptor sequence
>456cA (length=160) Species: 9606 (Homo sapiens) [Search protein sequence]
TLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDG
IADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTS
SSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDV
QGIQSLYGPG
3D structure
PDB456c Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors.
ChainA
Resolution2.4 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) H113 E114 H117 H123
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 H113 H117 H123
BS02 ZN A H172 D174 H187 H200 H63 D65 H78 H91
BS03 CA A D179 G180 P181 S182 L184 D202 E205 D70 G71 P72 S73 L75 D93 E96
BS04 CBP A L184 L185 A186 L218 H222 E223 H226 H232 L239 F241 P242 I243 Y244 T245 L75 L76 A77 L109 H113 E114 H117 H123 L130 F132 P133 I134 Y135 T136 MOAD: Ki=0.17nM
PDBbind-CN: -logKd/Ki=9.77,Ki=0.17nM
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:456c, PDBe:456c, PDBj:456c
PDBsum456c
PubMed10074939
UniProtP45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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