Structure of PDB 2mze Chain A

Receptor sequence
>2mzeA (length=250) Species: 9606 (Homo sapiens) [Search protein sequence]
LPLPQEAGGMSELQWEQAQDYLKRFYLYDSETKNANSLEAKLKEMQKFFG
LPITGMLNSRVIEIMQKPRCGVPDVAEYSLFPNSPKWTSKVVTYRIVSYT
RDLPHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSY
PFDGPGNTLAHAFAPGTGLGGDAHFDEDERWTDGSSLGINFLYAATHALG
HSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYGKRSNSRKK
3D structure
PDB2mze Charge-Triggered Membrane Insertion of Matrix Metalloproteinase-7, Supporter of Innate Immunity and Tumors.
ChainA
ResolutionN/A
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) H194 A195 H198 H204
Catalytic site (residue number reindexed from 1) H197 A198 H201 H207
Enzyme Commision number 3.4.24.23: matrilysin.
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 D133 G165 L166 G167 G168 D169 D136 G168 L169 G170 G171 D172
BS02 CA A D150 G151 P152 G153 N154 T155 D173 E176 D153 G154 P155 G156 N157 T158 D176 E179
BS03 ZN A H143 D145 H158 H171 H146 D148 H161 H174
BS04 ZN A C67 H194 H198 H204 C70 H197 H201 H207
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004222 metalloendopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0002779 antibacterial peptide secretion
GO:0002780 antibacterial peptide biosynthetic process
GO:0006508 proteolysis
GO:0006509 membrane protein ectodomain proteolysis
GO:0009410 response to xenobiotic stimulus
GO:0022617 extracellular matrix disassembly
GO:0030198 extracellular matrix organization
GO:0030335 positive regulation of cell migration
GO:0030574 collagen catabolic process
GO:0031293 membrane protein intracellular domain proteolysis
GO:0042127 regulation of cell population proliferation
GO:0042742 defense response to bacterium
GO:0050829 defense response to Gram-negative bacterium
GO:0050830 defense response to Gram-positive bacterium
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0031012 extracellular matrix
GO:0070062 extracellular exosome

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2mze, PDBe:2mze, PDBj:2mze
PDBsum2mze
PubMed26439767
UniProtP09237|MMP7_HUMAN Matrilysin (Gene Name=MMP7)

[Back to BioLiP]