eF-site ID 6n1k-ABCD PDB Code 6n1k Chain A, B, C, D click to enlarge Title Full-length human phenylalanine hydroxylase (PAH) in the resting state Classification OXIDOREDUCTASE Compound Phenylalanine-4-hydroxylase Source (PH4H_HUMAN) Sequence A:  ETSYIEDNQNGAISLIFSLKEEVGALAKVLRLFEENDVNL THIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDI GATVHELSRDKKKDTVPWFPRTIQELDRFANQILLDADHP GFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTW GTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQL EDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQ YIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIG LASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGL LSSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYY VAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLDNT QQLKILADSINSEIGILCS B:  QETSYIEDNSNGAISLIFSLKEEVGALAKVLRLFEENDVN LTHIESRPSRLKKDEYEFFTHLRSLPALTNIIKILRHDIT VHELSRDKKKDTVPWFPRTIQELDRFANQILSELDADHPG FKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWG TVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLE DVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQY IRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGL ASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLL SSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYV AESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLDNTQ QLKILADSINSEIGILCSAL C:  TSYIEDNSNQNGAISLIFSLKEEVGALAKVLRLFEENDVN LTHIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHD IGATVHELSRDKKKDTVPWFPRTIQELDRFANQILELDAD HPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKK TWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIP QLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHC TQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQE IGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGA GLLSSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPL YYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLD NTQQLKILADSINSEIGILCSAL D:  QETSYIEDNSGAISLIFSLKEEVGALAKVLRLFEENDTHI ESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDITVH ELSRDKKKDTVPWFPRTIQELDRFANQIELDADHPGFKDP VYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFK TLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQ FLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHG SKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLG APDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFG ELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESF NDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLDNTQQLKI LADSINSEIGILCS Description Functional site 1) chain A residue 297 type sequence R description binding site for residue CL A 501 source : AC1 2) chain A residue 285 type sequence H description binding site for residue FE A 502 source : AC2 3) chain A residue 290 type sequence H description binding site for residue FE A 502 source : AC2 4) chain A residue 330 type sequence E description binding site for residue FE A 502 source : AC2 5) chain A residue 71 type sequence R description binding site for residue CL B 501 source : AC3 6) chain B residue 297 type sequence R description binding site for residue CL B 501 source : AC3 7) chain B residue 285 type sequence H description binding site for residue FE B 502 source : AC4 8) chain B residue 290 type sequence H description binding site for residue FE B 502 source : AC4 9) chain B residue 330 type sequence E description binding site for residue FE B 502 source : AC4 10) chain C residue 261 type sequence R description binding site for residue CL C 501 source : AC5 11) chain C residue 297 type sequence R description binding site for residue CL C 501 source : AC5 12) chain C residue 301 type sequence Q description binding site for residue CL C 501 source : AC5 13) chain D residue 417 type sequence Y description binding site for residue CL C 501 source : AC5 14) chain C residue 285 type sequence H description binding site for residue FE C 502 source : AC6 15) chain C residue 290 type sequence H description binding site for residue FE C 502 source : AC6 16) chain C residue 330 type sequence E description binding site for residue FE C 502 source : AC6 17) chain D residue 297 type sequence R description binding site for residue CL D 501 source : AC7 18) chain D residue 301 type sequence Q description binding site for residue CL D 501 source : AC7 19) chain D residue 285 type sequence H description binding site for residue FE D 502 source : AC8 20) chain D residue 290 type sequence H description binding site for residue FE D 502 source : AC8 21) chain D residue 330 type sequence E description binding site for residue FE D 502 source : AC8 22) chain A residue 285 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P04176 source Swiss-Prot : SWS_FT_FI1 23) chain D residue 285 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P04176 source Swiss-Prot : SWS_FT_FI1 24) chain D residue 290 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P04176 source Swiss-Prot : SWS_FT_FI1 25) chain D residue 330 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P04176 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 290 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P04176 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 330 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P04176 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 285 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P04176 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 290 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P04176 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 330 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P04176 source Swiss-Prot : SWS_FT_FI1 31) chain C residue 285 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P04176 source Swiss-Prot : SWS_FT_FI1 32) chain C residue 290 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P04176 source Swiss-Prot : SWS_FT_FI1 33) chain C residue 330 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P04176 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 281-292 type prosite sequence PDICHELLGHVP description BH4_AAA_HYDROXYL_1 Biopterin-dependent aromatic amino acid hydroxylases signature. PDicHELLGHVP source prosite : PS00367

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