eF-site ID 4l8u-A PDB Code 4l8u Chain A click to enlarge Title X-ray study of human serum albumin complexed with 9 amino camptothecin Classification TRANSPORT PROTEIN Compound Serum albumin Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens; Sequence A:  AHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVK LVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLR ETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVD VMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRY KAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCA SLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKV HTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEK PLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAE AKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCC AAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEY KFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHP EAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESL VNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKER QIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKA DDKETCFAEEGKKLVAASQAALG Description (1)  Serum albumin Functional site 1) chain A residue 23 type sequence V description BINDING SITE FOR RESIDUE MYR A 601 source : AC1 2) chain A residue 150 type sequence Y description BINDING SITE FOR RESIDUE MYR A 601 source : AC1 3) chain A residue 254 type sequence A description BINDING SITE FOR RESIDUE MYR A 601 source : AC1 4) chain A residue 257 type sequence R description BINDING SITE FOR RESIDUE MYR A 601 source : AC1 5) chain A residue 284 type sequence L description BINDING SITE FOR RESIDUE MYR A 601 source : AC1 6) chain A residue 287 type sequence S description BINDING SITE FOR RESIDUE MYR A 601 source : AC1 7) chain A residue 342 type sequence S description BINDING SITE FOR RESIDUE MYR A 602 source : AC2 8) chain A residue 344 type sequence V description BINDING SITE FOR RESIDUE MYR A 602 source : AC2 9) chain A residue 348 type sequence R description BINDING SITE FOR RESIDUE MYR A 602 source : AC2 10) chain A residue 430 type sequence L description BINDING SITE FOR RESIDUE MYR A 602 source : AC2 11) chain A residue 453 type sequence L description BINDING SITE FOR RESIDUE MYR A 602 source : AC2 12) chain A residue 485 type sequence R description BINDING SITE FOR RESIDUE MYR A 602 source : AC2 13) chain A residue 391 type sequence N description BINDING SITE FOR RESIDUE MYR A 603 source : AC3 14) chain A residue 410 type sequence R description BINDING SITE FOR RESIDUE MYR A 603 source : AC3 15) chain A residue 411 type sequence Y description BINDING SITE FOR RESIDUE MYR A 603 source : AC3 16) chain A residue 418 type sequence V description BINDING SITE FOR RESIDUE MYR A 603 source : AC3 17) chain A residue 423 type sequence L description BINDING SITE FOR RESIDUE MYR A 603 source : AC3 18) chain A residue 460 type sequence L description BINDING SITE FOR RESIDUE MYR A 603 source : AC3 19) chain A residue 488 type sequence F description BINDING SITE FOR RESIDUE MYR A 603 source : AC3 20) chain A residue 401 type sequence Y description BINDING SITE FOR RESIDUE MYR A 604 source : AC4 21) chain A residue 525 type sequence K description BINDING SITE FOR RESIDUE MYR A 604 source : AC4 22) chain A residue 528 type sequence A description BINDING SITE FOR RESIDUE MYR A 604 source : AC4 23) chain A residue 529 type sequence L description BINDING SITE FOR RESIDUE MYR A 604 source : AC4 24) chain A residue 579 type sequence S description BINDING SITE FOR RESIDUE MYR A 604 source : AC4 25) chain A residue 210 type sequence A description BINDING SITE FOR RESIDUE MYR A 605 source : AC5 26) chain A residue 213 type sequence A description BINDING SITE FOR RESIDUE MYR A 605 source : AC5 27) chain A residue 324 type sequence D description BINDING SITE FOR RESIDUE MYR A 605 source : AC5 28) chain A residue 327 type sequence L description BINDING SITE FOR RESIDUE MYR A 605 source : AC5 29) chain A residue 482 type sequence V description BINDING SITE FOR RESIDUE MYR A 605 source : AC5 30) chain A residue 115 type sequence L description BINDING SITE FOR RESIDUE 9AZ A 606 source : AC6 31) chain A residue 117 type sequence R description BINDING SITE FOR RESIDUE 9AZ A 606 source : AC6 32) chain A residue 142 type sequence I description BINDING SITE FOR RESIDUE 9AZ A 606 source : AC6 33) chain A residue 146 type sequence H description BINDING SITE FOR RESIDUE 9AZ A 606 source : AC6 34) chain A residue 149 type sequence F description BINDING SITE FOR RESIDUE 9AZ A 606 source : AC6 35) chain A residue 182 type sequence L description BINDING SITE FOR RESIDUE 9AZ A 606 source : AC6 36) chain A residue 186 type sequence R description BINDING SITE FOR RESIDUE 9AZ A 606 source : AC6 37) chain A residue 189 type sequence G description BINDING SITE FOR RESIDUE 9AZ A 606 source : AC6 38) chain A residue 193 type sequence S description BINDING SITE FOR RESIDUE 9AZ A 606 source : AC6 39) chain A residue 161-185 type prosite sequence YKAAFTECCQAADKAACLLPKLDEL description ALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL source prosite : PS00212 40) chain A residue 353-377 type prosite sequence YETTLEKCCAAADPHECYAKVFDEF description ALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL source prosite : PS00212 41) chain A residue 551-575 type prosite sequence FAAFVEKCCKADDKETCFAEEGKKL description ALBUMIN_1 Albumin domain signature. YkaafteCCqaAdkaaCLlpkldeL source prosite : PS00212 42) chain A residue 3 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P02770 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 6 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P02769 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 252 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P02769 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 255 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P02769 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 259 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P02769 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 13 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P02769 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 244 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P02769 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 67 type BINDING sequence H description BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF source Swiss-Prot : SWS_FT_FI3 50) chain A residue 247 type BINDING sequence H description BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF source Swiss-Prot : SWS_FT_FI3 51) chain A residue 249 type BINDING sequence D description BINDING => ECO:0000269|PubMed:28567254, ECO:0007744|PDB:5IJF source Swiss-Prot : SWS_FT_FI3 52) chain A residue 240 type BINDING sequence K description BINDING => ECO:0000269|PubMed:656055 source Swiss-Prot : SWS_FT_FI4 53) chain A residue 174 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 54) chain A residue 181 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 55) chain A residue 190 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 56) chain A residue 195 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 57) chain A residue 205 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 58) chain A residue 212 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 59) chain A residue 240 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 60) chain A residue 262 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 61) chain A residue 274 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 62) chain A residue 286 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 63) chain A residue 20 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 64) chain A residue 359 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 65) chain A residue 372 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 66) chain A residue 389 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 67) chain A residue 402 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 68) chain A residue 414 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 69) chain A residue 432 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 70) chain A residue 436 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 71) chain A residue 466 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 72) chain A residue 475 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 73) chain A residue 500 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 74) chain A residue 41 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 75) chain A residue 519 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 76) chain A residue 524 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 77) chain A residue 538 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 78) chain A residue 541 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 79) chain A residue 557 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 80) chain A residue 560 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 81) chain A residue 564 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 82) chain A residue 574 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 83) chain A residue 64 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 84) chain A residue 73 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 85) chain A residue 93 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 86) chain A residue 106 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 87) chain A residue 136 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 88) chain A residue 159 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 89) chain A residue 4 type SITE sequence K description Not glycated => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI5 90) chain A residue 199 type SITE sequence K description Aspirin-acetylated lysine source Swiss-Prot : SWS_FT_FI6 91) chain A residue 5 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI7 92) chain A residue 58 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 93) chain A residue 65 type MOD_RES sequence S description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9 94) chain A residue 83 type MOD_RES sequence T description Phosphothreonine; by FAM20C => ECO:0000269|PubMed:26091039 source Swiss-Prot : SWS_FT_FI10 95) chain A residue 436 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P07724 source Swiss-Prot : SWS_FT_FI11 96) chain A residue 519 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P07724 source Swiss-Prot : SWS_FT_FI11 97) chain A residue 564 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P07724 source Swiss-Prot : SWS_FT_FI11 98) chain A residue 205 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P07724 source Swiss-Prot : SWS_FT_FI11 99) chain A residue 273 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P07724 source Swiss-Prot : SWS_FT_FI12 100) chain A residue 419 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI13 101) chain A residue 420 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI14 102) chain A residue 422 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI14 103) chain A residue 489 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI15 104) chain A residue 534 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315 source Swiss-Prot : SWS_FT_FI16 105) chain A residue 317 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977 source Swiss-Prot : SWS_FT_FI17 106) chain A residue 439 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977 source Swiss-Prot : SWS_FT_FI17 107) chain A residue 12 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977 source Swiss-Prot : SWS_FT_FI17 108) chain A residue 281 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:3759977 source Swiss-Prot : SWS_FT_FI17 109) chain A residue 444 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI18 110) chain A residue 536 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI18 111) chain A residue 545 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI18 112) chain A residue 573 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI18 113) chain A residue 137 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI18 114) chain A residue 162 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI18 115) chain A residue 225 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI18 116) chain A residue 276 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI18 117) chain A residue 313 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI18 118) chain A residue 323 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI18 119) chain A residue 378 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI18 120) chain A residue 413 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI18 121) chain A residue 51 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:15047055 source Swiss-Prot : SWS_FT_FI18 122) chain A residue 199 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6853480 source Swiss-Prot : SWS_FT_FI19 123) chain A residue 233 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977 source Swiss-Prot : SWS_FT_FI20 124) chain A residue 351 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977 source Swiss-Prot : SWS_FT_FI20 125) chain A residue 318 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine; in variant Redhill source Swiss-Prot : SWS_FT_FI21 126) chain A residue 494 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine; in variant Casebrook source Swiss-Prot : SWS_FT_FI22 127) chain A residue 525 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine => ECO:0000269|PubMed:15047055, ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6706980, ECO:0000269|PubMed:6853480 source Swiss-Prot : SWS_FT_FI23 128) chain A residue 534 type CARBOHYD sequence K description N-linked (Glc) (glycation) lysine; alternate => ECO:0000269|PubMed:3759977 source Swiss-Prot : SWS_FT_FI24

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