eF-site ID 1m9c-ABCD PDB Code 1m9c Chain A, B, C, D click to enlarge Title X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type Complex. Classification Isomerase/Viral protein Compound Cyclophilin A Source null (Q72497_9HIV1) Sequence A:  MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALS TGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYG EKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTE WLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIAD CGQLE B:  NPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTG EKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEK FEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWL DGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCG QLE C:  PIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMF SALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEW DRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTH NPPIPVGEIYKRWIILGLNKIVRMYS D:  VHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQ DLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGP IAPGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIY KRWIILGLNKIVRMYS Description Functional site 1) chain A residue 1 type MOD_RES sequence M 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 2) chain A residue 2 type MOD_RES sequence V 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 3) chain A residue 28 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 4) chain A residue 82 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 5) chain B residue 28 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 6) chain B residue 82 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 7) chain A residue 44 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 8) chain A residue 76 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 9) chain A residue 131 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 10) chain B residue 44 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 11) chain B residue 76 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 12) chain B residue 131 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 13) chain A residue 77 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 14) chain B residue 77 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 15) chain A residue 93 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI6 16) chain B residue 93 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI6 17) chain A residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 18) chain B residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 19) chain A residue 133 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17742 source Swiss-Prot : SWS_FT_FI8 20) chain B residue 133 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17742 source Swiss-Prot : SWS_FT_FI8 21) chain A residue 108 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 22) chain B residue 108 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 23) chain A residue 28 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate source Swiss-Prot : SWS_FT_FI10 24) chain B residue 28 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate source Swiss-Prot : SWS_FT_FI10 25) chain A residue 82 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI11 26) chain B residue 82 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI11 27) chain A residue 55 type catalytic sequence R description 189 source MCSA : MCSA1 28) chain A residue 60 type catalytic sequence F description 189 source MCSA : MCSA1 29) chain A residue 63 type catalytic sequence Q description 189 source MCSA : MCSA1 30) chain A residue 102 type catalytic sequence N description 189 source MCSA : MCSA1 31) chain A residue 113 type catalytic sequence F description 189 source MCSA : MCSA1 32) chain A residue 122 type catalytic sequence L description 189 source MCSA : MCSA1 33) chain A residue 126 type catalytic sequence H description 189 source MCSA : MCSA1 34) chain B residue 55 type catalytic sequence R description 189 source MCSA : MCSA2 35) chain B residue 60 type catalytic sequence F description 189 source MCSA : MCSA2 36) chain B residue 63 type catalytic sequence Q description 189 source MCSA : MCSA2 37) chain B residue 102 type catalytic sequence N description 189 source MCSA : MCSA2 38) chain B residue 113 type catalytic sequence F description 189 source MCSA : MCSA2 39) chain B residue 122 type catalytic sequence L description 189 source MCSA : MCSA2 40) chain B residue 126 type catalytic sequence H description 189 source MCSA : MCSA2 41) 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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