Dimeric structure of FIH (Factor inhibiting HIF)

Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau.

MAATAAEAVTSGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEY
LQENIGNGDFSVYSASTHKFLYYDEKK(MSE)ANFQNFKPRSNREE(MSE)KFHEFVEKLQDIQQRGGEERLYLQQTLND
TVGGKIV(MSE)DFLGFNWNWINKQQGKRGWGQLTSNLLLIG(MSE)EGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQF
ECLYPYPVHHPCDRQSQVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIP(MSE)YWWHHIESLLNGGITITVNFWYKGA
PTPKRIEYPLKAHQKVAI(MSE)RNIEK(MSE)LGEALGNPQEVGPLLNT(MSE)IKGRYN

MAATAAEAVTSGSGEPREEAGALGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEY
LQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNREEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGGKIVM
DFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQS
QVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMR
NIEKMLGEALGNPQEVGPLLNTMIKGRYN

0.4M Lithium sulfate, 20% PEG 4000, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

The second part of the biological assembly is generated by the two fold axis : -x, y, -z

MAATAAEAVTSGSGEPREEAGALGPAWHESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEY
LQENIGNGDFSVYSASTHKFLYYDEKKMANFQNFKPRSNREEMKFHEFVEKLQDIQQRGGEERLYLQQTLNDTVGGKIVM
DFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGYKRCILFPPDQFECLYPYPVHHPCDRQS
QVDFDNPDYERFPNFQNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMR
NIEKMLGEALGNPQEVGPLLNTMIKGRYN