eF-site ID 4yun-A PDB Code 4yun Chain A click to enlarge Title Multiconformer synchrotron model of CypA at 310 K Classification ISOMERASE Compound Peptidyl-prolyl cis-trans isomerase A Source Homo sapiens (Human) (PPIA_HUMAN) Sequence A:  VNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALST GEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGE KFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEW LDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADC GQL Description Functional site 1) chain A residue 55 type catalytic sequence R description 189 source MCSA : MCSA1 2) chain A residue 60 type catalytic sequence F description 189 source MCSA : MCSA1 3) chain A residue 63 type catalytic sequence Q description 189 source MCSA : MCSA1 4) chain A residue 102 type catalytic sequence N description 189 source MCSA : MCSA1 5) chain A residue 113 type catalytic sequence F description 189 source MCSA : MCSA1 6) chain A residue 122 type catalytic sequence L description 189 source MCSA : MCSA1 7) chain A residue 126 type catalytic sequence H description 189 source MCSA : MCSA1 8) chain A residue 28 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 82 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 10) 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 11) 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 12) 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 13) 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 14) chain A residue 44 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 15) chain A residue 76 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 16) chain A residue 131 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 17) chain A residue 77 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 18) chain A residue 93 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI6 19) 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 20) chain A 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

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