Structure of PDB 5ue5 Chain A Binding Site BS06
Receptor Information
>5ue5 Chain A (length=247) Species:
9606
(Homo sapiens) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
PQEAGGMSELQWEQAQDYLKRFYLYDSETKNANSLEAKLKEMQKFFGLPI
TGMLNSRVIEIMQKPRCGVPDVAEYSLFPNSPKWTSKVVTYRIVSYTRDL
PHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFD
GPGNTLAHAFAPGTGLGGDAHFDEDERWTDGSSLGINFLYAATHALGHSL
GMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYGKRSNSRKK
Ligand information
Ligand ID
CA
InChI
InChI=1S/Ca/q+2
InChIKey
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
Formula
Ca
Name
CALCIUM ION
ChEMBL
DrugBank
DB14577
ZINC
PDB chain
5ue5 Chain A Residue 302 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
5ue5
Glycan Activation of a Sheddase: Electrostatic Recognition between Heparin and proMMP-7.
Resolution
N/A
Binding residue
(original residue number in PDB)
D150 G151 P152 G153 N154 T155 D173 E176
Binding residue
(residue number reindexed from 1)
D150 G151 P152 G153 N154 T155 D173 E176
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
H194 A195 H198 H204
Catalytic site (residue number reindexed from 1)
H194 A195 H198 H204
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
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:5ue5
,
PDBe:5ue5
,
PDBj:5ue5
PDBsum
5ue5
PubMed
28648610
UniProt
P09237
|MMP7_HUMAN Matrilysin (Gene Name=MMP7)
[
Back to BioLiP
]