Structure of PDB 5cuh Chain A

Receptor sequence

>5cuhA (length=164) Species: 9606 (Homo sapiens)

GFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLT
FTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFD
DDELWSLGKGVGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPP
LHKDDVNGIRHLYG

3D structure

• PDB: 5cuh Discovery of a new selective inhibitor of A Disintegrin And Metalloprotease 10 (ADAM-10) able to reduce the shedding of NKG2D ligands in Hodgkin's lymphoma cell models.
• Chain: A
• Resolution: 1.83 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H226 E227 H230 H236
• Catalytic site (residue number reindexed from 1): H121 E122 H125 H131
• Enzyme Commision number: 3.4.24.35: gelatinase B.

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	H226 H230 H236	H121 H125 H131
BS02	ZN	A	H175 D177 H190 H203	H70 D72 H85 H98
BS03	CA	A	D165 G197 Q199 D201	D60 G92 Q94 D96
BS04	CA	A	D131 D206 E208	D26 D101 E103
BS05	CA	A	D182 G183 D185 L187 D205 E208	D77 G78 D80 L82 D100 E103
BS06	LTQ	A	L187 L188 L222 H226 E227 H230 H236 L243 M247 Y248	L82 L83 L117 H121 E122 H125 H131 L138 M142 Y143	PDBbind-CN: -logKd/Ki=4.62,IC50=24uM BindingDB: IC50=24000nM

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

External links

• PDB: RCSB:5cuh, PDBe:5cuh, PDBj:5cuh
• PDBsum: 5cuh
• PubMed: 26871660
• UniProt: P14780|MMP9_HUMAN Matrix metalloproteinase-9 (Gene Name=MMP9)