Structure of PDB 456c Chain B

Receptor sequence
>456cB (length=159) Species: 9606 (Homo sapiens) [Search protein sequence]
LKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGI
ADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSS
SKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQ
GIQSLYGPG
3D structure
PDB456c Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors.
ChainB
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) H112 E113 H116 H122
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 H112 H116 H122
BS02 ZN B H172 D174 H187 H200 H62 D64 H77 H90
BS03 CA B D179 G180 P181 S182 L184 D202 E205 D69 G70 P71 S72 L74 D92 E95
BS04 CBP B A186 L218 H222 E223 H226 H232 L239 F241 P242 I243 Y244 T245 A76 L108 H112 E113 H116 H122 L129 F131 P132 I133 Y134 T135 MOAD: 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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Molecular Function
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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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