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●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

Structure of PDB 4c2p Chain A Binding Site BS04

Receptor Information >4c2p Chain A (length=582) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] DEAEASKFVEEYDRTSQVVWNEYAEANWNYNTNITTETSKILLQKNMQIA NHTLKYGTQARKFDVNQLQNTTIKRIIKKVQDLERAALPAQELEEYNKIL LDMETTYSVATVCHPNGSCLQLEPDLTNVMATSRKYEDLLWAWEGWRDKA GRAILQFYPKYVELINQAARLNGYVDAGDSWRSMYETPSLEQDLERLFQE LQPLYLNLHAYVRRALHRHYGAQHINLEGPIPAHLLGNMWAQTWSNIYDL VVPFPSAPSMDTTEAMLKQGWTPRRMFKEADDFFTSLGLLPVPPEFWNKS MLEKPTDGREVVCHASAWDFYNGKDFRIKQCTTVNLEDLVVAHHEMGHIQ YFMQYKDLPVALREGANPGFHEAIGDVLALSVSTPKHLHSLNLLSSDEHD INFLMKMALDKIAFIPFSYLVDQWRWRVFDGSITKENYNQEWWSLRLKYQ GLCPPVPRTQGDFDPGAKFHIPSSVPYIKYFVSFIIQFQFHEALCQAAGH TGPLHKCDIYQSKEAGQRLATAMKLGFSRPWPEAMQLITGQPNMSASAML SYFKPLLDWLRTENELHGEKLGWPQYNWTPNS

Ligand information Ligand ID CL InChI InChI=1S/ClH/h1H/p-1 InChIKey VEXZGXHMUGYJMC-UHFFFAOYSA-M SMILES Software SMILES ACDLabs 10.04 CACTVS 3.341 OpenEye OEToolkits 1.5.0 [Cl-] Formula Cl Name CHLORIDE ION ChEMBL DrugBank DB14547 ZINC PDB chain 4c2p Chain A Residue 703 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 4c2p Molecular and Thermodynamic Mechanisms of the Chloride Dependent Human Angiotensin-I Converting Enzyme (Ace) Resolution 1.99 Å Binding residue (original residue number in PDB) Y224 P407 K522 Binding residue (residue number reindexed from 1) Y185 P368 K479 Annotation score 1

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

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