Structure of PDB 1jj9 Chain A

Receptor sequence
>1jj9A (length=158) Species: 9606 (Homo sapiens) [Search protein sequence]
NPKWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQG
EADINIAFYQRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDAEETWTN
TSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDI
DGIQAIYG
3D structure
PDB1jj9 The 1.8-A crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H197 E198 H201 H207
Catalytic site (residue number reindexed from 1) H113 E114 H117 H123
Enzyme Commision number 3.4.24.34: neutrophil collagenase.
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 CA A D137 G169 G171 D173 D53 G85 G87 D89
BS02 CA A D154 G155 N157 I159 D177 E180 D70 G71 N73 I75 D93 E96
BS03 ZN A H147 D149 H162 H175 H63 D65 H78 H91
BS04 ZN A H197 H201 H207 H113 H117 H123
BS05 BBT A L160 A161 H197 E198 H201 H207 P217 N218 L76 A77 H113 E114 H117 H123 P133 N134 MOAD: ic50=1700nM
PDBbind-CN: -logKd/Ki=5.77,IC50=1.7uM
BindingDB: IC50=1700nM
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:1jj9, PDBe:1jj9, PDBj:1jj9
PDBsum1jj9
PubMed11278347
UniProtP22894|MMP8_HUMAN Neutrophil collagenase (Gene Name=MMP8)

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