eF-site ID 6njj-ABCD PDB Code 6njj Chain A, B, C, D click to enlarge Title Crystal Structure of the PDE4D Catalytic Domain and UCR2 Regulatory Helix with BPN14770 Classification HYDROLASE/HYDROLASE INHIBITOR Compound cAMP-specific 3',5'-cyclic phosphodiesterase 4D Source (PDE4D_HUMAN) Sequence A:  QEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQ ERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAAD VVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGV SNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCD IFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMV ETKKVTVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYR QWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQV GFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTI PNQVSEFISNTFLD B:  QEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQ ERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAAD VVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGV SNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCD IFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMV ETKKVTVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYR QWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQV GFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTI PNQVSEFISNTFLD C:  QEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQ ERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAAD VVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGV SNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCD IFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMV ETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQ LYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEK SQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQ STIPNQVSEFISNTFLD D:  QEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQ ERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAAD VVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGV SNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCD IFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMV ETKKVTVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYR QWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQV GFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTI PNQVSEFISNTFLD Description Functional site 1) chain A residue 330 type sequence H description binding site for residue ZN A 701 source : AC1 2) chain A residue 366 type sequence H description binding site for residue ZN A 701 source : AC1 3) chain A residue 367 type sequence D description binding site for residue ZN A 701 source : AC1 4) chain A residue 484 type sequence D description binding site for residue ZN A 701 source : AC1 5) chain A residue 367 type sequence D description binding site for residue MG A 702 source : AC2 6) chain A residue 325 type sequence Y description binding site for residue KR7 A 703 source : AC3 7) chain A residue 439 type sequence M description binding site for residue KR7 A 703 source : AC3 8) chain A residue 487 type sequence N description binding site for residue KR7 A 703 source : AC3 9) chain A residue 495 type sequence Y description binding site for residue KR7 A 703 source : AC3 10) chain A residue 498 type sequence W description binding site for residue KR7 A 703 source : AC3 11) chain A residue 499 type sequence T description binding site for residue KR7 A 703 source : AC3 12) chain A residue 502 type sequence I description binding site for residue KR7 A 703 source : AC3 13) chain A residue 535 type sequence Q description binding site for residue KR7 A 703 source : AC3 14) chain A residue 538 type sequence F description binding site for residue KR7 A 703 source : AC3 15) chain A residue 599 type sequence F description binding site for residue KR7 A 703 source : AC3 16) chain A residue 603 type sequence T description binding site for residue KR7 A 703 source : AC3 17) chain A residue 318 type sequence H description binding site for residue BTB A 704 source : AC4 18) chain A residue 409 type sequence E description binding site for residue BTB A 704 source : AC4 19) chain C residue 320 type sequence H description binding site for residue BTB A 704 source : AC4 20) chain C residue 322 type sequence D description binding site for residue BTB A 704 source : AC4 21) chain C residue 369 type sequence D description binding site for residue BTB A 704 source : AC4 22) chain C residue 371 type sequence P description binding site for residue BTB A 704 source : AC4 23) chain C residue 512 type sequence R description binding site for residue BTB A 704 source : AC4 24) chain A residue 318 type sequence H description binding site for residue ZN A 705 source : AC5 25) chain A residue 271 type sequence H description binding site for residue SO4 A 706 source : AC6 26) chain A residue 272 type sequence V description binding site for residue SO4 A 706 source : AC6 27) chain A residue 273 type sequence F description binding site for residue SO4 A 706 source : AC6 28) chain A residue 274 type sequence R description binding site for residue SO4 A 706 source : AC6 29) chain A residue 494 type sequence L description binding site for residue SO4 A 706 source : AC6 30) chain A residue 497 type sequence Q description binding site for residue SO4 A 706 source : AC6 31) chain A residue 341 type sequence L description binding site for residue EDO A 707 source : AC7 32) chain A residue 344 type sequence T description binding site for residue EDO A 707 source : AC7 33) chain A residue 550 type sequence W description binding site for residue EDO A 707 source : AC7 34) chain A residue 557 type sequence D description binding site for residue EDO A 707 source : AC7 35) chain A residue 561 type sequence I description binding site for residue EDO A 707 source : AC7 36) chain B residue 330 type sequence H description binding site for residue ZN B 701 source : AC8 37) chain B residue 366 type sequence H description binding site for residue ZN B 701 source : AC8 38) chain B residue 367 type sequence D description binding site for residue ZN B 701 source : AC8 39) chain B residue 484 type sequence D description binding site for residue ZN B 701 source : AC8 40) chain B residue 367 type sequence D description binding site for residue MG B 702 source : AC9 41) chain B residue 325 type sequence Y description binding site for residue KR7 B 703 source : AD1 42) chain B residue 439 type sequence M description binding site for residue KR7 B 703 source : AD1 43) chain B residue 487 type sequence N description binding site for residue KR7 B 703 source : AD1 44) chain B residue 495 type sequence Y description binding site for residue KR7 B 703 source : AD1 45) chain B residue 498 type sequence W description binding site for residue KR7 B 703 source : AD1 46) chain B residue 499 type sequence T description binding site for residue KR7 B 703 source : AD1 47) chain B residue 502 type sequence I description binding site for residue KR7 B 703 source : AD1 48) chain B residue 535 type sequence Q description binding site for residue KR7 B 703 source : AD1 49) chain B residue 538 type sequence F description binding site for residue KR7 B 703 source : AD1 50) chain B residue 599 type sequence F description binding site for residue KR7 B 703 source : AD1 51) chain B residue 271 type sequence H description binding site for residue SO4 B 704 source : AD2 52) chain B residue 272 type sequence V description binding site for residue SO4 B 704 source : AD2 53) chain B residue 273 type sequence F description binding site for residue SO4 B 704 source : AD2 54) chain B residue 274 type sequence R description binding site for residue SO4 B 704 source : AD2 55) chain B residue 493 type sequence Q description binding site for residue SO4 B 704 source : AD2 56) chain B residue 494 type sequence L description binding site for residue SO4 B 704 source : AD2 57) chain B residue 497 type sequence Q description binding site for residue SO4 B 704 source : AD2 58) chain C residue 330 type sequence H description binding site for residue ZN C 701 source : AD3 59) chain C residue 366 type sequence H description binding site for residue ZN C 701 source : AD3 60) chain C residue 367 type sequence D description binding site for residue ZN C 701 source : AD3 61) chain C residue 484 type sequence D description binding site for residue ZN C 701 source : AD3 62) chain C residue 367 type sequence D description binding site for residue MG C 702 source : AD4 63) chain C residue 325 type sequence Y description binding site for residue KR7 C 703 source : AD5 64) chain C residue 439 type sequence M description binding site for residue KR7 C 703 source : AD5 65) chain C residue 487 type sequence N description binding site for residue KR7 C 703 source : AD5 66) chain C residue 495 type sequence Y description binding site for residue KR7 C 703 source : AD5 67) chain C residue 498 type sequence W description binding site for residue KR7 C 703 source : AD5 68) chain C residue 499 type sequence T description binding site for residue KR7 C 703 source : AD5 69) chain C residue 502 type sequence I description binding site for residue KR7 C 703 source : AD5 70) chain C residue 535 type sequence Q description binding site for residue KR7 C 703 source : AD5 71) chain C residue 538 type sequence F description binding site for residue KR7 C 703 source : AD5 72) chain C residue 599 type sequence F description binding site for residue KR7 C 703 source : AD5 73) chain C residue 271 type sequence H description binding site for residue SO4 C 704 source : AD6 74) chain C residue 272 type sequence V description binding site for residue SO4 C 704 source : AD6 75) chain C residue 273 type sequence F description binding site for residue SO4 C 704 source : AD6 76) chain C residue 274 type sequence R description binding site for residue SO4 C 704 source : AD6 77) chain C residue 493 type sequence Q description binding site for residue SO4 C 704 source : AD6 78) chain C residue 494 type sequence L description binding site for residue SO4 C 704 source : AD6 79) chain C residue 497 type sequence Q description binding site for residue SO4 C 704 source : AD6 80) chain D residue 330 type sequence H description binding site for residue ZN D 701 source : AD7 81) chain D residue 366 type sequence H description binding site for residue ZN D 701 source : AD7 82) chain D residue 367 type sequence D description binding site for residue ZN D 701 source : AD7 83) chain D residue 484 type sequence D description binding site for residue ZN D 701 source : AD7 84) chain D residue 367 type sequence D description binding site for residue MG D 702 source : AD8 85) chain D residue 325 type sequence Y description binding site for residue KR7 D 703 source : AD9 86) chain D residue 439 type sequence M description binding site for residue KR7 D 703 source : AD9 87) chain D residue 487 type sequence N description binding site for residue KR7 D 703 source : AD9 88) chain D residue 495 type sequence Y description binding site for residue KR7 D 703 source : AD9 89) chain D residue 498 type sequence W description binding site for residue KR7 D 703 source : AD9 90) chain D residue 499 type sequence T description binding site for residue KR7 D 703 source : AD9 91) chain D residue 502 type sequence I description binding site for residue KR7 D 703 source : AD9 92) chain D residue 535 type sequence Q description binding site for residue KR7 D 703 source : AD9 93) chain D residue 538 type sequence F description binding site for residue KR7 D 703 source : AD9 94) chain D residue 599 type sequence F description binding site for residue KR7 D 703 source : AD9 95) chain B residue 320 type sequence H description binding site for residue BTB D 704 source : AE1 96) chain B residue 322 type sequence D description binding site for residue BTB D 704 source : AE1 97) chain D residue 318 type sequence H description binding site for residue BTB D 704 source : AE1 98) chain D residue 409 type sequence E description binding site for residue BTB D 704 source : AE1 99) chain D residue 318 type sequence H description binding site for residue ZN D 705 source : AE2 100) chain D residue 271 type sequence H description binding site for residue SO4 D 706 source : AE3 101) chain D residue 272 type sequence V description binding site for residue SO4 D 706 source : AE3 102) chain D residue 273 type sequence F description binding site for residue SO4 D 706 source : AE3 103) chain D residue 274 type sequence R description binding site for residue SO4 D 706 source : AE3 104) chain D residue 494 type sequence L description binding site for residue SO4 D 706 source : AE3 105) chain D residue 497 type sequence Q description binding site for residue SO4 D 706 source : AE3 106) chain A residue 366-377 type prosite sequence HDVDHPGVSNQF description PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDVdHpGvsNqF source prosite : PS00126 107) chain A residue 387 type ACT_SITE sequence L description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 108) chain B residue 387 type ACT_SITE sequence L description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 109) chain C residue 387 type ACT_SITE sequence L description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 110) chain D residue 387 type ACT_SITE sequence L description Proton donor => ECO:0000250|UniProtKB:Q07343 source Swiss-Prot : SWS_FT_FI1 111) chain A residue 391 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI3 112) chain B residue 391 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI3 113) chain C residue 391 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI3 114) chain D residue 391 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI3 115) chain A residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI4 116) chain B residue 427 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI4 117) chain B residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI4 118) chain C residue 427 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI4 119) chain C residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI4 120) chain D residue 427 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI4 121) chain D residue 545 type BINDING sequence P description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI4 122) chain A residue 427 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0000269|PubMed:15576036, ECO:0000269|PubMed:17582435, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7, ECO:0007744|PDB:1TBB, ECO:0007744|PDB:1XOM, ECO:0007744|PDB:1XON, ECO:0007744|PDB:1XOQ, ECO:0007744|PDB:1XOR, ECO:0007744|PDB:2PW3 source Swiss-Prot : SWS_FT_FI4 123) chain A residue 428 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 124) chain B residue 428 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 125) chain C residue 428 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 126) chain D residue 428 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14609333, ECO:0007744|PDB:1PTW source Swiss-Prot : SWS_FT_FI5 127) chain A residue 300 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 128) chain C residue 273 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 129) chain C residue 300 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 130) chain D residue 273 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 131) chain D residue 300 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 132) chain A residue 273 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 133) chain B residue 273 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 134) chain B residue 300 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 135) chain A residue 312 type CROSSLNK sequence L description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI7 136) chain B residue 312 type CROSSLNK sequence L description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI7 137) chain C residue 312 type CROSSLNK sequence L description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI7 138) chain D residue 312 type CROSSLNK sequence L description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) source Swiss-Prot : SWS_FT_FI7 139) chain C residue 387 type BINDING sequence L description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 140) chain C residue 548 type BINDING sequence E description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 141) chain D residue 387 type BINDING sequence L description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 142) chain D residue 548 type BINDING sequence E description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 143) chain A residue 387 type BINDING sequence L description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 144) chain A residue 548 type BINDING sequence E description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 145) chain B residue 387 type BINDING sequence L description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2 146) chain B residue 548 type BINDING sequence E description BINDING => ECO:0000269|PubMed:14609333, ECO:0000269|PubMed:15260978, ECO:0007744|PDB:1PTW, ECO:0007744|PDB:1TB7 source Swiss-Prot : SWS_FT_FI2

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