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BioLiP

Structure of PDB 1bkc Chain E

Receptor sequence
>1bkcE (length=256) Species: 9606 (Homo sapiens) [Search protein sequence]
DPMKNTCKLLVVADHRFYRYMGRGEESTTTNYLIELIDRVDDIYRNTAWD
NAGFKGYGIQIEQIRILKSPQEVKPGEKHYNMAKSYPNEEKDAWDVKMLL
EQFSFDIAEEASKVCLAHLFTYQDFDMGTLGLAYVGSPRANSHGGVCPKA
YYSPVGKKNIYLNSGLTSTKNYGKTILTKEADLVTTHELGHNFGAEHDPD
GKAECAPNEDQGGKYVMYPIAVSGDHENNKMFSQCSKQSIYKTIESKAQE
CFQERS
3D structure
PDB1bkc Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme.
ChainE
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.24.86: ADAM 17 endopeptidase.
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 E H405 H409 H415 H187 H191 H197
BS02 INN E G346 T347 L348 G349 H405 E406 H415 P437 I438 A439 G128 T129 L130 G131 H187 E188 H197 P219 I220 A221
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0008237 metallopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:1bkc, PDBe:1bkc, PDBj:1bkc
PDBsum1bkc
PubMed9520379
UniProtP78536|ADA17_HUMAN Disintegrin and metalloproteinase domain-containing protein 17 (Gene Name=ADAM17)

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