eF-site ID 2b0u-ABCD PDB Code 2b0u Chain A, B, C, D click to enlarge Title The Structure of the Follistatin:Activin Complex Classification SIGNALING PROTEIN Compound Inhibin beta A chain Source Homo sapiens (Human) (FST_HUMAN) Sequence A:  GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYC EGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSC CVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS B:  GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYC EGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSC CVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS C:  GNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEED VNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPGKKCRMN KKNKPRCVCAPDCSNITKGPVCGLDGKTYRNECALLKARC KEQPELEVQYQGRCKKTCRDVFCPGSSTCVVDQTNNAYCV TCNRICPEPASSEQYLCGNDGVTYSSACHLRKATCLLGRS IGLAYEGKCIKAKSCEDIQCTGGKKCLWDFKVGRGRCSLC DELCPDSKSDEPVCASDNATYASECAMKEAACSSGVLLEV KHSGSCN D:  GNCWLRQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEED VNDNTLFKWMIFNGGAPNCIPCKETCENVDCGPKCRMNKK NKPRCVCAPDCSNKGPVCGLDGKTYRNECALLKARCKEQP ELEVQYQGRCKKTCRDVFCPGSSTCVVDQTNNAYCVTCNR ICPEPSSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLAY EGKCIKAKSCEDIQCTGGKKCLWDFKVGRGRCSLCDELCP DSDEPVCASDNATYASECAMKEAACSSGVLLEVKHSGSCN Description (1)  The Structure of the Follistatin:Activin Complex Functional site 1) chain B residue 15 type sequence Q description BINDING SITE FOR RESIDUE IR3 B 502 source : AC1 2) chain C residue 282 type sequence K description BINDING SITE FOR RESIDUE IR3 C 503 source : AC2 3) chain C residue 48 type sequence K description BINDING SITE FOR RESIDUE IR3 C 505 source : AC3 4) chain C residue 261 type sequence T description BINDING SITE FOR RESIDUE MLI C 400 source : AC4 5) chain A residue 17 type sequence F description BINDING SITE FOR RESIDUE MLI A 401 source : AC5 6) chain A residue 21 type sequence K description BINDING SITE FOR RESIDUE MLI A 402 source : AC6 7) chain A residue 22 type sequence D description BINDING SITE FOR RESIDUE MLI A 402 source : AC6 8) chain C residue 167 type sequence C description BINDING SITE FOR RESIDUE MLI A 402 source : AC6 9) chain C residue 190 type sequence H description BINDING SITE FOR RESIDUE MLI A 402 source : AC6 10) chain C residue 193 type sequence K description BINDING SITE FOR RESIDUE MLI A 402 source : AC6 11) chain A residue 32 type sequence P description BINDING SITE FOR RESIDUE MLI A 403 source : AC7 12) chain A residue 90 type sequence S description BINDING SITE FOR RESIDUE MLI A 403 source : AC7 13) chain D residue 105 type sequence L description BINDING SITE FOR RESIDUE MLI A 403 source : AC7 14) chain D residue 106 type sequence D description BINDING SITE FOR RESIDUE MLI A 403 source : AC7 15) chain B residue 31 type sequence A description BINDING SITE FOR RESIDUE MPD B 404 source : AC8 16) chain B residue 32 type sequence P description BINDING SITE FOR RESIDUE MPD B 404 source : AC8 17) chain B residue 90 type sequence S description BINDING SITE FOR RESIDUE MPD B 404 source : AC8 18) chain B residue 91 type sequence M description BINDING SITE FOR RESIDUE MPD B 404 source : AC8 19) chain C residue 105 type sequence L description BINDING SITE FOR RESIDUE MPD B 404 source : AC8 20) chain C residue 106 type sequence D description BINDING SITE FOR RESIDUE MPD B 404 source : AC8 21) chain C residue 126 type sequence E description BINDING SITE FOR RESIDUE MPD B 404 source : AC8 22) chain A residue 29-44 type prosite sequence IIAPSGYHANYCEGEC description TGF_BETA_1 TGF-beta family signature. IiaPsgYhanyCeGeC source prosite : PS00250 23) chain C residue 95 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 24) chain C residue 259 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 25) chain D residue 95 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 26) chain D residue 259 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI1

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