Structure of PDB 1fm1 Chain A

Receptor sequence
>1fm1A (length=158) Species: 9606 (Homo sapiens) [Search protein sequence]
TLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDG
IADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTS
SSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDV
QGIQSLYG
3D structure
PDB1fm1 High-resolution solution structure of the catalytic fragment of human collagenase-3 (MMP-13) complexed with a hydroxamic acid inhibitor.
ChainA
ResolutionN/A
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H119 E120 H123 H129
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 H119 H123 H129 H113 H117 H123
BS02 ZN A H69 H84 H97 H63 H78 H91
BS03 CA A D76 G77 P78 S79 G80 L81 D99 E102 D70 G71 P72 S73 G74 L75 D93 E96
BS04 WAY A G80 L81 L82 H119 H123 H129 P139 Y141 G74 L75 L76 H113 H117 H123 P133 Y135 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:1fm1, PDBe:1fm1, PDBj:1fm1
PDBsum1fm1
PubMed10986126
UniProtP45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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