Structure of PDB 2iux Chain A

Receptor sequence
>2iuxA (length=577) Species: 9606 (Homo sapiens) [Search protein sequence]
DEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIA
NHTLKYGTQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKIL
LDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKA
GRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQE
LQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDL
VVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWQKS
MLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQ
YFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSGGSD
EHDINFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRL
KYQGLCPPVPRTQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCQA
AGHTGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPQMSAS
AMLSYFKPLLDWLRTENELHGEKLGWP
3D structure
PDB2iux Structure of Testis Ace Glycosylation Mutants and Evidence for Conserved Domain Movement.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H353 A354 H383 E384 H387 E411 H513 Y523
Catalytic site (residue number reindexed from 1) H314 A315 H344 E345 H348 E372 H473 Y483
Enzyme Commision number 3.4.15.1: peptidyl-dipeptidase A.
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 H383 H387 E411 H344 H348 E372
BS02 CL A R186 W486 R489 R147 W446 R449
BS03 CL A Y224 P407 R522 Y185 P368 R482
BS04 NXA A H353 H513 Y523 H314 H473 Y483
Gene Ontology
Molecular Function
GO:0008237 metallopeptidase activity
GO:0008241 peptidyl-dipeptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2iux, PDBe:2iux, PDBj:2iux
PDBsum2iux
PubMed17042482
UniProtP12821|ACE_HUMAN Angiotensin-converting enzyme (Gene Name=ACE)

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