Structure of PDB 5ue4 Chain B

Receptor sequence

>5ue4B (length=220) Species: 9606 (Homo sapiens)

DRQLAEEYLYRYGYTRVAESLGPALLLLQKQLSLPETGELDSATLKAMRT
PRCGVPDLGRFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWS
AVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQ
GDAHFDDDELWSLGKGQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYR
FTEGPPLHKDDVNGIRHLYG

3D structure

• PDB: 5ue4 Discovery of a highly selective chemical inhibitor of matrix metalloproteinase-9 (MMP-9) that allosterically inhibits zymogen activation.
• Chain: B
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H226 E227 H230 H236
• Catalytic site (residue number reindexed from 1): H177 E178 H181 H187
• 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	B	C99 H226 H230 H236	C53 H177 H181 H187
BS02	ZN	B	H175 D177 H190 H203	H126 D128 H141 H154
BS03	CA	B	D182 G183 D185 L187 D205 E208	D133 G134 D136 L138 D156 E159
BS04	CA	B	D165 G197 Q199 D201	D116 G148 Q150 D152
BS05	5XQ	B	V101 P102 R106 F110 L114 Y179 H190 A191 F192 P193 H230 G233 L234	V55 P56 R60 F61 L65 Y130 H141 A142 F143 P144 H181 G184 L185	MOAD: Kd=3.3uM PDBbind-CN: -logKd/Ki=6.36,IC50=440nM

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:5ue4, PDBe:5ue4, PDBj:5ue4
• PDBsum: 5ue4
• PubMed: 28860188
• UniProt: P14780|MMP9_HUMAN Matrix metalloproteinase-9 (Gene Name=MMP9)