Structure of PDB 5n5k Chain A

Receptor sequence

>5n5kA (length=156) Species: 9606 (Homo sapiens)

VWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMA
DILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHS
GGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRG
IQSLYG

3D structure

• PDB: 5n5k Lipoyl-Homotaurine Derivative (ADM_12) Reverts Oxaliplatin-Induced Neuropathy and Reduces Cancer Cells Malignancy by Inhibiting Carbonic Anhydrase IX (CAIX).
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H218 E219 H222 H228
• Catalytic site (residue number reindexed from 1): H111 E112 H115 H121
• Enzyme Commision number: 3.4.24.65: macrophage elastase.

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	H218 H222 H228	H111 H115 H121
BS02	ZN	A	H168 D170 H183 H196	H61 D63 H76 H89
BS03	CA	A	D158 G190 G192 D194	D51 G83 G85 D87
BS04	CA	A	D124 E199 E201	D17 E92 E94
BS05	CA	A	D175 G176 G178 I180 D198 E201	D68 G69 G71 I73 D91 E94
BS06	8NW	A	L181 L214 T215 H218 E219 F237 P238 T239 Y240 K241	L74 L107 T108 H111 E112 F130 P131 T132 Y133 K134

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:5n5k, PDBe:5n5k, PDBj:5n5k
• PDBsum: 5n5k
• PubMed: 29048889
• UniProt: P39900|MMP12_HUMAN Macrophage metalloelastase (Gene Name=MMP12)