eF-site ID 4zel-AB PDB Code 4zel Chain A, B Title Human dopamine beta-hydroxylase Classification OXIDOREDUCTASE Compound Dopamine beta-hydroxylase Source Homo sapiens (Human) (DOPO_HUMAN) Sequence A:  PLPYHIPLDPEGSLELSWNVSYTQEAIHFQLLVRRLKAGV LFGMSDRGELENADLVVLWTDGDAYFADAWSDQKGQIHLD PQQDYQLLQVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTV HLVYGILEEPFRSLEAINGSGLQMGLQRVQLLKPNIPEPE LPSDACTMEVQAPNIQIPSQETTYWCYIKELPKGFSRHHI IKYEPIVTKGNEALVHHMEVFQCAPEMDSVPHFSGPCDSK MKPDRLNYCRHVLAAWALGAKAFYYPEEAGLAFGGPGSSR YLRLEVHYHNPLVIEGRNDSSGIRLYYTAKLRRFNAGIME LGLVYTPVMAIPPRETAFILTGYCTDKCTQLALPPSGIHI FASQLHTHLTGRKVVTVLVRDGREWEIVNQDNHYSPHFQE IRMLKKVVSVHPGDVLITSCTYNTEDRELATVGGFGILEE MCVNYVHYYPQTQLELCKSAVDAGFLQKYFHLINRFNNED VCTCPQASVSQQFTSVPWNSFNRDVLKALYSFAPISMHCN KSSAVRFQGEWNLQPLPKVISTLEEPTVVS B:  PLPYHIPLDPEGSLELSWNVSYTQEAIHFQLLVRRLKAGV LFGMSDRGELENADLVVLAYFADAWSDQKGQIHLDPQQDY QLLQVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYG ILEEPFRSLEAINGSGLQMGLQRVQLLKPNIPEPELPSDA CTMEVQAPNIQIPSQETTYWCYIKELPKGFSRHHIIKYEP IVTKGNEALVHHMEVFQCAPEVPHFSGPCDSKMLNYCRHV LAAWALGAKAFYYPEEAGLAFGGPGSSRYLRLEVHYHNPL VIEGRNDSSGIRLYYTAKLRRFNAGIMELGLVYTPVMAIP PRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGR KVVTVLVRDGREWEIVNQDNHYSPHFQEIRMLKKVVSVHP GDVLITSCTYNTEDRELATVGGFGILEEMCVNYVHYYPQT QLELCKSAVDAGFLQKYFHLINRFNNEDVCTCPQASVSQQ FTSVPWNSFNRDVLKALYSFAPISMHCNKSSAVRFQGEWN LQPLPKVISTLEEPTPQCVVSIGG Description (1)  dopamine beta hydroxylase Functional site 1) chain A residue 191 type ACT_SITE ligand sequence G description {ECO:0000255}. source Swiss-Prot : SWS_FT_FI1 2) chain A residue 373 type ACT_SITE ligand sequence P description {ECO:0000255}. source Swiss-Prot : SWS_FT_FI1 3) chain A residue 223 type METAL ligand sequence I description Copper A. {ECO:0000250} source Swiss-Prot : SWS_FT_FI2 4) chain A residue 224 type METAL ligand sequence P description Copper A. {ECO:0000250} source Swiss-Prot : SWS_FT_FI2 5) chain A residue 294 type METAL ligand sequence Y description Copper A. {ECO:0000250} source Swiss-Prot : SWS_FT_FI2 6) chain A residue 373 type METAL ligand sequence P description Copper B. {ECO:0000250} source Swiss-Prot : SWS_FT_FI3 7) chain A residue 375 type METAL ligand sequence M description Copper B. {ECO:0000250} source Swiss-Prot : SWS_FT_FI3 8) chain A residue 448 type METAL ligand sequence R description Copper B. {ECO:0000250} source Swiss-Prot : SWS_FT_FI3 9) chain B residue 191 type ACT_SITE ligand sequence G description {ECO:0000255}. source Swiss-Prot : SWS_FT_FI5 10) chain B residue 373 type ACT_SITE ligand sequence P description {ECO:0000255}. source Swiss-Prot : SWS_FT_FI5 11) chain B residue 223 type METAL ligand sequence I description Copper A. {ECO:0000250} source Swiss-Prot : SWS_FT_FI6 12) chain B residue 224 type METAL ligand sequence P description Copper A. {ECO:0000250} source Swiss-Prot : SWS_FT_FI6 13) chain B residue 294 type METAL ligand sequence Y description Copper A. {ECO:0000250} source Swiss-Prot : SWS_FT_FI6 14) chain B residue 373 type METAL ligand sequence P description Copper B. {ECO:0000250} source Swiss-Prot : SWS_FT_FI7 15) chain B residue 375 type METAL ligand sequence M description Copper B. {ECO:0000250} source Swiss-Prot : SWS_FT_FI7 16) chain B residue 448 type METAL ligand sequence R description Copper B. {ECO:0000250} source Swiss-Prot : SWS_FT_FI7 17) chain A residue 262-269 type prosite ligand sequence HHMEVFQC description Copper type II, ascorbate-dependent monooxygenases signature 1.H-H-M-x(2)-F-x-C. source prosite : PS00084 18) chain B residue 262-269 type prosite ligand sequence HHMEVFQC description Copper type II, ascorbate-dependent monooxygenases signature 1.H-H-M-x(2)-F-x-C. source prosite : PS00084 19) chain A residue 405-417 type prosite ligand sequence HIFASQLHTHLTG description Copper type II, ascorbate-dependent monooxygenases signature 2.H-x-F-x(4)-H-T-H-x(2)-G. source prosite : PS00085 20) chain B residue 405-417 type prosite ligand sequence HIFASQLHTHLTG description Copper type II, ascorbate-dependent monooxygenases signature 2.H-x-F-x(4)-H-T-H-x(2)-G. source prosite : PS00085

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