eF-site ID 4zel-AB PDB Code 4zel Chain A, B click to enlarge 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 412 type BINDING sequence H description BINDING => ECO:0000269|PubMed:27152332, ECO:0007744|PDB:4ZEL source Swiss-Prot : SWS_FT_FI3 2) chain A residue 487 type BINDING sequence M description BINDING => ECO:0000269|PubMed:27152332, ECO:0007744|PDB:4ZEL source Swiss-Prot : SWS_FT_FI3 3) chain B residue 412 type BINDING sequence H description BINDING => ECO:0000269|PubMed:27152332, ECO:0007744|PDB:4ZEL source Swiss-Prot : SWS_FT_FI3 4) chain B residue 487 type BINDING sequence M description BINDING => ECO:0000269|PubMed:27152332, ECO:0007744|PDB:4ZEL source Swiss-Prot : SWS_FT_FI3 5) chain A residue 64 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:27152332, ECO:0007744|PDB:4ZEL source Swiss-Prot : SWS_FT_FI4 6) chain A residue 344 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:27152332, ECO:0007744|PDB:4ZEL source Swiss-Prot : SWS_FT_FI4 7) chain A residue 566 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:27152332, ECO:0007744|PDB:4ZEL source Swiss-Prot : SWS_FT_FI4 8) chain B residue 64 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:27152332, ECO:0007744|PDB:4ZEL source Swiss-Prot : SWS_FT_FI4 9) chain B residue 344 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:27152332, ECO:0007744|PDB:4ZEL source Swiss-Prot : SWS_FT_FI4 10) chain B residue 566 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:27152332, ECO:0007744|PDB:4ZEL source Swiss-Prot : SWS_FT_FI4 11) chain A residue 262 type BINDING sequence H description BINDING => ECO:0000305|PubMed:27152332 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 263 type BINDING sequence H description BINDING => ECO:0000305|PubMed:27152332 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 333 type BINDING sequence H description BINDING => ECO:0000305|PubMed:27152332 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 414 type BINDING sequence H description BINDING => ECO:0000305|PubMed:27152332 source Swiss-Prot : SWS_FT_FI2 15) chain B residue 262 type BINDING sequence H description BINDING => ECO:0000305|PubMed:27152332 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 263 type BINDING sequence H description BINDING => ECO:0000305|PubMed:27152332 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 333 type BINDING sequence H description BINDING => ECO:0000305|PubMed:27152332 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 414 type BINDING sequence H description BINDING => ECO:0000305|PubMed:27152332 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 230 type ACT_SITE sequence Y description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 412 type ACT_SITE sequence H description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 230 type ACT_SITE sequence Y description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 412 type ACT_SITE sequence H description ACT_SITE => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 184 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:27152332, ECO:0007744|PDB:4ZEL source Swiss-Prot : SWS_FT_FI5 24) chain B residue 184 type CARBOHYD sequence N description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:27152332, ECO:0007744|PDB:4ZEL source Swiss-Prot : SWS_FT_FI5 25) chain A residue 262-269 type prosite sequence HHMEVFQC description CU2_MONOOXYGENASE_1 Copper type II, ascorbate-dependent monooxygenases signature 1. HHMevFqC source prosite : PS00084 26) chain A residue 405-417 type prosite sequence HIFASQLHTHLTG description CU2_MONOOXYGENASE_2 Copper type II, ascorbate-dependent monooxygenases signature 2. HiFasqlHTHltG source prosite : PS00085

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