Structure of PDB 3hhs Chain B

Receptor sequence
>3hhsB (length=656) Species: 7130 (Manduca sexta) [Search protein sequence]
DAKNNLLYFFDRPNEPCFMQKGEDKVVFEIPDHYYPDKYKSLSNTLSNRF
GNEATKRIPIRNITLPNLEVPMQLPYNDQFSLFVPKHRTMAAKLIDIFMG
MRDVEDLQSVCSYCQLRINPYMFNYCLSVAILHRPDTKGLSIPTFAETFP
DKFMDSKVFLRAREVSNVVISGSRMPVNVPINYTANTTEPEQRVAYFRED
IGINLHHWHWHLVYPFDSADRSIVNKDRRGELFYYMHQQIIGRYNVERMC
NGLPQVKPFSDFSAPIEEGYFPKLDSQVASRTWPPRFAGSVFRNLDRTVD
QVKIDVRKLFTWRDQFLEAIQKMAIKMPNGRELPLDEVTGIDMLGNLMES
SIISPNRGYYGDLHNMGHVFAAYTHDPDHRHLEQFGVMGDSATAMRDPFF
YRWHRFVDDVFNIYKEKLTPYTNERLDFPGVRVSSVGIEGRPNTLRTLWQ
QSTVELGRGLDFTPRGSVLARFTHLQHDEFQYVIEVNNTTGGNLMGTVRI
FMAPKVDDNGQPMSFNKQRRLMIELDKFSQALRPGTNTIRRRSVDSSVTI
PYERTDFCGCGWPHHMLIPKGTAQGYPVVLFVMISNWNNDRIEQDGSCND
AASYCGIRDRKYPDKQAMGYPFDRKMANDAATLSDFLRPNMAVRDCSIQF
SDTTVE
3D structure
PDB3hhs Crystal structure of Manduca sexta prophenoloxidase provides insights into the mechanism of type 3 copper enzymes.
ChainB
Resolution1.97 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.18.1: tyrosinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CU B H366 H370 H406 H364 H368 H404
BS02 CU B H209 H213 H239 H207 H211 H237
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0004503 tyrosinase activity
GO:0005507 copper ion binding
GO:0016491 oxidoreductase activity
GO:0031404 chloride ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006582 melanin metabolic process
GO:0006583 melanin biosynthetic process from tyrosine
GO:0006952 defense response
GO:0035008 positive regulation of melanization defense response
GO:0042438 melanin biosynthetic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3hhs, PDBe:3hhs, PDBj:3hhs
PDBsum3hhs
PubMed19805072
UniProtO44249|PRP1_MANSE Phenoloxidase subunit 1

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