eF-site ID 2ilm-AS PDB Code 2ilm Chain A, S click to enlarge Title Factor Inhibiting HIF-1 Alpha D201A Mutant in Complex with FE(II), Alpha-Ketoglutarate and HIF-1 Alpha 35mer Classification TRANSCRIPTION REGULATOR, OXIDOREDUCTASE Compound Hypoxia-inducible factor 1 alpha inhibitor Source Homo sapiens (Human) (HIF1A_HUMAN) Sequence A:  AVASGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQ SDPRAEELIENEEPVVLTDTNLVYPALKWDLEYLQENIGN GDFSVYSASTHKFLYYDEKKMANFQNFKPRSNREEMKFHE FVEKLQDIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNW NWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYAEQQNFF AQIKGYKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNP DYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNG GITITVNFWYKGAPTPKIEYPLKAHQKVAIMRNIEKMLGE ALGNPQEVGPLLNTMIKGRYN S:  QLTSYD Description Functional site 1) chain A residue 199 type sequence H description BINDING SITE FOR RESIDUE FE2 A 350 source : AC1 2) chain A residue 279 type sequence H description BINDING SITE FOR RESIDUE FE2 A 350 source : AC1 3) chain A residue 140 type sequence G description BINDING SITE FOR RESIDUE SO4 A 1352 source : AC2 4) chain A residue 141 type sequence E description BINDING SITE FOR RESIDUE SO4 A 1352 source : AC2 5) chain A residue 142 type sequence E description BINDING SITE FOR RESIDUE SO4 A 1352 source : AC2 6) chain A residue 107 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1353 source : AC3 7) chain A residue 237 type sequence D description BINDING SITE FOR RESIDUE SO4 A 1353 source : AC3 8) chain A residue 320 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1353 source : AC3 9) chain A residue 199 type sequence H description BINDING SITE FOR RESIDUE BCT A 3000 source : AC4 10) chain A residue 201 type sequence A description BINDING SITE FOR RESIDUE BCT A 3000 source : AC4 11) chain A residue 238 type sequence R description BINDING SITE FOR RESIDUE BCT A 3000 source : AC4 12) chain A residue 279 type sequence H description BINDING SITE FOR RESIDUE BCT A 3000 source : AC4 13) chain A residue 296 type sequence W description BINDING SITE FOR RESIDUE BCT A 3000 source : AC4 14) chain A residue 145 type sequence Y description BINDING SITE FOR RESIDUE AKG A 1351 source : AC5 15) chain A residue 188 type sequence L description BINDING SITE FOR RESIDUE AKG A 1351 source : AC5 16) chain A residue 196 type sequence T description BINDING SITE FOR RESIDUE AKG A 1351 source : AC5 17) chain A residue 199 type sequence H description BINDING SITE FOR RESIDUE AKG A 1351 source : AC5 18) chain A residue 205 type sequence N description BINDING SITE FOR RESIDUE AKG A 1351 source : AC5 19) chain A residue 207 type sequence F description BINDING SITE FOR RESIDUE AKG A 1351 source : AC5 20) chain A residue 214 type sequence K description BINDING SITE FOR RESIDUE AKG A 1351 source : AC5 21) chain A residue 279 type sequence H description BINDING SITE FOR RESIDUE AKG A 1351 source : AC5 22) chain A residue 281 type sequence I description BINDING SITE FOR RESIDUE AKG A 1351 source : AC5 23) chain A residue 294 type sequence N description BINDING SITE FOR RESIDUE AKG A 1351 source : AC5 24) chain A residue 296 type sequence W description BINDING SITE FOR RESIDUE AKG A 1351 source : AC5 25) chain A residue 10 type sequence A description BINDING SITE FOR RESIDUE GOL A 2001 source : AC6 26) chain A residue 37 type sequence F description BINDING SITE FOR RESIDUE GOL A 2001 source : AC6 27) chain A residue 38 type sequence P description BINDING SITE FOR RESIDUE GOL A 2001 source : AC6 28) chain A residue 150 type sequence L description BINDING SITE FOR RESIDUE GOL A 2002 source : AC7 29) chain A residue 151 type sequence N description BINDING SITE FOR RESIDUE GOL A 2002 source : AC7 30) chain A residue 152 type sequence D description BINDING SITE FOR RESIDUE GOL A 2002 source : AC7 31) chain A residue 89 type sequence D description BINDING SITE FOR RESIDUE GOL A 2003 source : AC8 32) chain A residue 148 type sequence Q description BINDING SITE FOR RESIDUE GOL A 2003 source : AC8 33) chain A residue 196 type MOD_RES sequence T description S-nitrosocysteine => ECO:0000305|PubMed:12914934 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 205 type MOD_RES sequence N description S-nitrosocysteine => ECO:0000305|PubMed:12914934 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 214 type MOD_RES sequence K description S-nitrosocysteine => ECO:0000305|PubMed:12914934 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 294 type MOD_RES sequence N description S-nitrosocysteine => ECO:0000305|PubMed:12914934 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 199 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12432100, ECO:0000269|PubMed:12446723, ECO:0000269|PubMed:15913349, ECO:0000269|PubMed:17135241, ECO:0000269|PubMed:20396966, ECO:0000269|PubMed:20822901, ECO:0000269|PubMed:21251231, ECO:0000269|PubMed:21460794 source Swiss-Prot : SWS_FT_FI3 38) chain A residue 201 type BINDING sequence A description BINDING => ECO:0000269|PubMed:12432100, ECO:0000269|PubMed:12446723, ECO:0000269|PubMed:15913349, ECO:0000269|PubMed:17135241, ECO:0000269|PubMed:20396966, ECO:0000269|PubMed:20822901, ECO:0000269|PubMed:21251231, ECO:0000269|PubMed:21460794 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 279 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12432100, ECO:0000269|PubMed:12446723, ECO:0000269|PubMed:15913349, ECO:0000269|PubMed:17135241, ECO:0000269|PubMed:20396966, ECO:0000269|PubMed:20822901, ECO:0000269|PubMed:21251231, ECO:0000269|PubMed:21460794 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 340 type SITE sequence L description Important for dimer formation source Swiss-Prot : SWS_FT_FI4 41) chain A residue 181 type MOD_RES sequence Q description (3S)-3-hydroxyasparagine => ECO:0000269|PubMed:12080085 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 238 type MOD_RES sequence R description (3S)-3-hydroxyasparagine => ECO:0000269|PubMed:12080085 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 300 type MOD_RES sequence A description (3S)-3-hydroxyasparagine => ECO:0000269|PubMed:12080085 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 321 type MOD_RES sequence N description (3S)-3-hydroxyasparagine => ECO:0000269|PubMed:12080085 source Swiss-Prot : SWS_FT_FI2

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