eF-site ID 1m9y-F PDB Code 1m9y Chain F click to enlarge Title X-ray crystal structure of Cyclophilin A/HIV-1 CA N-terminal domain (1-146) M-type H87A,G89A Complex. Classification Isomerase/Viral protein Compound Cyclophilin A Source Homo sapiens (Human) (Q72497_9HIV1) Sequence F:  VNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALST GEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGE KFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEW LDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADC GQLE Description Functional site 1) chain F residue 55 type catalytic sequence R description 189 source MCSA : MCSA4 2) chain F residue 60 type catalytic sequence F description 189 source MCSA : MCSA4 3) chain F residue 63 type catalytic sequence Q description 189 source MCSA : MCSA4 4) chain F residue 102 type catalytic sequence N description 189 source MCSA : MCSA4 5) chain F residue 113 type catalytic sequence F description 189 source MCSA : MCSA4 6) chain F residue 122 type catalytic sequence L description 189 source MCSA : MCSA4 7) chain F residue 126 type catalytic sequence H description 189 source MCSA : MCSA4 8) chain F 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 9) chain F 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 10) chain F 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 11) chain F residue 28 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 12) chain F residue 82 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 13) chain F residue 44 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 14) chain F residue 76 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 15) chain F residue 131 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 16) chain F residue 77 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 17) chain F residue 93 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI6 18) chain F 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 F residue 133 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P17742 source Swiss-Prot : SWS_FT_FI8 20) chain F residue 108 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI9

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