Structure of PDB 1umt Chain A

Receptor sequence
>1umtA (length=166) Species: 9606 (Homo sapiens) [Search protein sequence]
FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTF
SRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDD
DEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRF
RLSQDDINGIQSLYGP
3D structure
PDB1umt Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic 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) H201 E202 H205 H211
Catalytic site (residue number reindexed from 1) H119 E120 H123 H129
Enzyme Commision number 3.4.24.17: stromelysin 1.
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 H201 H205 H211 H119 H123 H129
BS02 ZN A H151 D153 H166 H179 H69 D71 H84 H97
BS03 CA A D158 G159 G161 N162 V163 L164 D181 E184 D76 G77 G79 N80 V81 L82 D99 E102
BS04 0DS A Y155 N162 V163 T191 L197 H201 H211 Y220 P221 L222 Y73 N80 V81 T109 L115 H119 H129 Y138 P139 L140 BindingDB: Ki=127nM
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:1umt, PDBe:1umt, PDBj:1umt
PDBsum1umt
PubMed8580839
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

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