eF-site ID 1cwo-A PDB Code 1cwo Chain A click to enlarge Title HUMAN CYCLOPHILIN A COMPLEXED WITH THR2, LEU5, D-HIV8, LEU10 CYCLOSPORIN Classification ISOMERASE/IMMUNOSUPPRESSANT Compound PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A Source null (NOR00035) Sequence A:  MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALS TGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTE WLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD CGQLE Description Functional site 1) chain A residue 19 type sequence R description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 2) chain A residue 55 type sequence R description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 3) chain A residue 60 type sequence F description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 4) chain A residue 63 type sequence Q description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 5) chain A residue 72 type sequence G description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 6) chain A residue 89 type sequence I description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 7) chain A residue 101 type sequence A description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 8) chain A residue 102 type sequence N description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 9) chain A residue 103 type sequence A description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 10) chain A residue 111 type sequence Q description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 11) chain A residue 113 type sequence F description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 12) chain A residue 121 type sequence W description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 13) chain A residue 126 type sequence H description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 14) chain A residue 163 type sequence Q description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 15) chain A residue 164 type sequence L description BINDING SITE FOR CHAIN C OF CYCLOSPORIN C source : AC1 16) chain A residue 56 type catalytic sequence I description 189 source MCSA : MCSA1 17) chain A residue 61 type catalytic sequence M description 189 source MCSA : MCSA1 18) chain A residue 64 type catalytic sequence G description 189 source MCSA : MCSA1 19) chain A residue 103 type catalytic sequence A description 189 source MCSA : MCSA1 20) chain A residue 114 type catalytic sequence I description 189 source MCSA : MCSA1 21) chain A residue 123 type catalytic sequence D description 189 source MCSA : MCSA1 22) chain A residue 127 type catalytic sequence V description 189 source MCSA : MCSA1 23) chain A residue 2 type MOD_RES sequence V description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 3 type MOD_RES sequence N description N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed => ECO:0000269|PubMed:25489052, ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI2 25) chain A residue 29 type MOD_RES sequence V description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 83 type MOD_RES sequence F description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 45 type MOD_RES sequence G description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 77 type MOD_RES sequence S description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 29) chain A residue 132 type MOD_RES sequence V description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 30) chain A residue 78 type MOD_RES sequence I description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 94 type MOD_RES sequence G description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI6 32) chain A residue 126 type MOD_RES sequence H description N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 33) chain A residue 134 type MOD_RES sequence E description N6-acetyllysine => ECO:0000250|UniProtKB:P17742 source Swiss-Prot : SWS_FT_FI8 34) chain A residue 109 type CARBOHYD sequence G description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 35) chain A residue 29 type CROSSLNK sequence V description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate source Swiss-Prot : SWS_FT_FI10 36) chain A residue 83 type CROSSLNK sequence F description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI11 37) chain A residue 48-65 type prosite sequence YKGSCFHRIIPGFMCQGG description CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgScFHRIIpgFMcQGG source prosite : PS00170

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