Structure of PDB 4xct Chain A

Receptor sequence

>4xctA (length=157) Species: 9606 (Homo sapiens)

DLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSR
DADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSL
GKGVGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVN
GIRHLYG

3D structure

• PDB: 4xct N-O-Isopropyl Sulfonamido-Based Hydroxamates as Matrix Metalloproteinase Inhibitors: Hit Selection and in Vivo Antiangiogenic Activity.
• Chain: A
• Resolution: 1.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H226 E227 H230 H236
• Catalytic site (residue number reindexed from 1): H114 E115 H118 H124
• 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	N73	A	L187 A189 L222 H226 E227 H230 H236 L243 Y245 P246 M247 Y248	L75 A77 L110 H114 E115 H118 H124 L131 Y133 P134 M135 Y136	MOAD: ic50=6.7nM PDBbind-CN: -logKd/Ki=8.17,IC50=6.7nM
BS02	ZN	A	H226 H230 H236	H114 H118 H124
BS03	ZN	A	H175 D177 H190 H203	H63 D65 H78 H91
BS04	CA	A	D182 G183 D185 L187 D205 E208	D70 G71 D73 L75 D93 E96
BS05	CA	A	D165 G197 Q199 D201	D53 G85 Q87 D89
BS06	CA	A	D131 D206 E208	D19 D94 E96
BS07	BUD	A	E130 L132	E18 L20

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:4xct, PDBe:4xct, PDBj:4xct
• PDBsum: 4xct
• PubMed: 26263024
• UniProt: P14780|MMP9_HUMAN Matrix metalloproteinase-9 (Gene Name=MMP9)