Structure of PDB 4apj Chain A Binding Site BS01

Receptor Information

>4apj Chain A (length=581) Species: 9606 (Homo sapiens)

DEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIA
NHTLKYGTQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKIL
LDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKA
GRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQE
LQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDL
VVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKS
MLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQ
YFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSDEHD
INFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQ
GLCPPVPRTQGDFDPGAKFHIPSSVPYIRYFVSFIIQFQFHEALCQAAGH
TGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAML
SYFKPLLDWLRTENELHGEKLGWPQYNWTPN

Ligand information

>4apj Chain P (length=11) Species: 242054 (Gloydius blomhoffii)

EGLPPRPKIPP

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4apj Molecular Recognition and Regulation of Human Angiotensin-I Converting Enzyme (Ace) Activity by Natural Inhibitory Peptides.
• Resolution: 2.6 Å
• Binding residue (original residue number in PDB): W59 K118 D121 E123 Q281 A354 S355 A356 W357 Y360 H387 E403 F457 K511 F512 H513 S517 Y520 Y523
• Binding residue (residue number reindexed from 1): W20 K79 D82 E84 Q242 A315 S316 A317 W318 Y321 H348 E364 F414 K468 F469 H470 S474 Y477 Y480

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 H470 Y480
• Enzyme Commision number: 3.4.15.1: peptidyl-dipeptidase A.

Gene Ontology

Molecular Function

• GO:0008237 metallopeptidase activity
• GO:0008241 peptidyl-dipeptidase activity

Biological Process

• GO:0006508 proteolysis

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:4apj, PDBe:4apj, PDBj:4apj
• PDBsum: 4apj
• PubMed: 23056909
• UniProt: P12821|ACE_HUMAN Angiotensin-converting enzyme (Gene Name=ACE)