Structure of PDB 2jsd Chain A

Receptor sequence
>2jsdA (length=160) Species: 9606 (Homo sapiens) [Search protein sequence]
GEPKWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINS
GEADIMISFENGDHGDSYPFDGPRGTLAHAFAPGEGLGGDTHFDNAEKWT
MGTNGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPYGFHLPKDD
VKGIQALYGP
3D structure
PDB2jsd Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase.
ChainA
ResolutionN/A
3D
structure
Catalytic site residues are labeled in the structure
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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.-
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 CA A D183 G184 R186 T188 D206 E209 D71 G72 R74 T76 D94 E97
BS02 CA A E164 A165 D166 E197 G198 D202 E52 A53 D54 E85 G86 D90
BS03 ZN A H176 D178 H191 H204 H64 D66 H79 H92
BS04 ZN A H226 H230 H236 H114 H118 H124
BS05 NGH A T188 L189 A190 H226 E227 H230 H236 P246 Y248 T76 L77 A78 H114 E115 H118 H124 P134 Y136 PDBbind-CN: -logKd/Ki=7.77,Kd=17nM
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:2jsd, PDBe:2jsd, PDBj:2jsd
PDBsum2jsd
PubMed17869250
UniProtO60882|MMP20_HUMAN Matrix metalloproteinase-20 (Gene Name=MMP20)

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