Structure of PDB 2mze Chain A Binding Site BS02

Receptor Information
>2mze Chain A (length=250) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LPLPQEAGGMSELQWEQAQDYLKRFYLYDSETKNANSLEAKLKEMQKFFG
LPITGMLNSRVIEIMQKPRCGVPDVAEYSLFPNSPKWTSKVVTYRIVSYT
RDLPHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSY
PFDGPGNTLAHAFAPGTGLGGDAHFDEDERWTDGSSLGINFLYAATHALG
HSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYGKRSNSRKK
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain2mze Chain A Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2mze Charge-Triggered Membrane Insertion of Matrix Metalloproteinase-7, Supporter of Innate Immunity and Tumors.
ResolutionN/A
Binding residue
(original residue number in PDB)		D150 G151 P152 G153 N154 T155 D173 E176
Binding residue
(residue number reindexed from 1)		D153 G154 P155 G156 N157 T158 D176 E179
Annotation score4
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.
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2mze, PDBe:2mze, PDBj:2mze
PDBsum2mze
PubMed26439767
UniProtP09237|MMP7_HUMAN Matrilysin (Gene Name=MMP7)

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