Structure of PDB 6klg Chain A

Receptor sequence
>6klgA (length=547) Species: 4577 (Zea mays) [Search protein sequence]
THYDFVITETKVTRLCHEKTILAVNGQFPGPTIYARKDDVVIVNVYNQGY
KNITLHWHGVDQPRNPWSDGPEYITQCPIQPGANFTYKIIFTEEEGTLWW
HAHSEFDRATVHGAIVIHPKRGTVYPYPKPHKEMPIILGEWWNADVEQIL
LESQRTGGDVNISDANTINGQPGDFAPCSKEDTFKMSVEHGKTYLLRVIN
AGLTNEMFFAVAGHRLTVVGTDGRYLRPFTVDYILISPGQTMNMLLEANC
ATDGSANSRYYMAARPFFTNTAVNVDDKNTTAIVEYTDAPPSASAGPPDS
PDLPAMDDIAAATAYTAQLRSLVTKEHPIDVPMEVDEHMLVTISVNTIPC
EPNKTCAGPGNNRLAASLNNVSFMNPTIDILDAYYDSISGVYEPDFPNKP
PFFFNFTAPNPPQDLWFTKRGTKVKVVEYGTILEVVFQDTAILGAESHPM
HLHGFSFYVVGRGFGNFDKDKDPATYNLVDPPYQNTVSVPTGGWAAMRFR
AANPGVWFMHCHFDRHTVWGMDTVFIVKNGKGPDAQMMPRPPNMPKC
3D structure
PDB6klg Structural basis for monolignol oxidation by a maize laccase.
ChainA
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.10.3.2: laccase.
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 A H451 C514 H519 H448 C511 H516
BS02 CU A H59 H454 H456 H56 H451 H453
BS03 CU A H106 H456 H513 H103 H453 H510
BS04 CU A H61 H104 H515 H58 H101 H512
BS05 OXY A H59 H104 H106 H454 H513 H515 H56 H101 H103 H451 H510 H512
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0052716 hydroquinone:oxygen oxidoreductase activity
Biological Process
GO:0046274 lignin catabolic process
Cellular Component
GO:0048046 apoplast

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6klg, PDBe:6klg, PDBj:6klg
PDBsum6klg
PubMed32123349
UniProtQ2PAJ1

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