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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