Structure of PDB 1caq Chain A

Receptor sequence
>1caqA (length=168) Species: 9606 (Homo sapiens) [Search protein sequence]
FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTF
SRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDD
DEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRF
RLSQDDINGIQSLYGPPP
3D structure
PDB1caq X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity.
ChainA
Resolution1.8 Å
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 V163 D181 E184 D76 G77 G79 V81 D99 E102
BS04 CA A D141 G173 N175 D177 D59 G91 N93 D95
BS05 CA A D107 D182 E184 D25 D100 E102
BS06 DPS A L164 A165 H201 E202 H205 H211 P221 L222 Y223 H224 L226 L82 A83 H119 E120 H123 H129 P139 L140 Y141 H142 L144 MOAD: Ki=19nM
PDBbind-CN: -logKd/Ki=7.72,Ki=19nM
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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Cellular Component
External links
PDB RCSB:1caq, PDBe:1caq, PDBj:1caq
PDBsum1caq
PubMed10422833
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

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