Structure of PDB 1uea Chain C

Receptor sequence
>1ueaC (length=168) Species: 9606 (Homo sapiens) [Search protein sequence]
FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTF
SRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDD
DEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRF
RLSQDDINGIQSLYGPPP
3D structure
PDB1uea Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1.
ChainC
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 C H201 H205 H211 H119 H123 H129
BS02 ZN C H151 D153 H166 H179 H69 D71 H84 H97
BS03 CA C D158 G159 G161 V163 D181 E184 D76 G77 G79 V81 D99 E102
BS04 CA C D141 G173 N175 D177 D59 G91 N93 D95
BS05 CA C D107 D182 D183 E184 Q185 D25 D100 D101 E102 Q103
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1uea, PDBe:1uea, PDBj:1uea
PDBsum1uea
PubMed9288970
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

[Back to BioLiP]