Structure of PDB 3njv Chain A

Receptor sequence
>3njvA (length=508) Species: 5053 (Aspergillus aculeatus) [Search protein sequence]
AFGITTSSSAYVIDTNAPNQLKFTVSRSSCDITSIIHYGTELQYSSQGSH
IGSGLGSATVTATQSGDYIKVTCVTDTLTQYMVVHNGDPIIHMATYITAE
PSIGELRFIARLNSDLLPNEEPFGDVSTTADGTAIEGSDVFLVGSETRSA
FYSSERFIDDQRHCIAGDAHRVCMILNQYESSSGGPFHRDINSNNGGSYN
ALYWYMNSGHVQTESYRMGLHGPYSMYFSRSGTPSTSIDTSFFADLDIKG
YVAASGRGKVAGTASGADSSMDWVVHWYNDAAQYWTYTSSSGSFTSPAMK
PGTYTMVYYQGEYAVATSSVTVSAGSTTTKNISGSVKTGTTIFKIGEWDG
QPTGFRNAANQLRMHPSDSRMSSWGPLTYTVGSSALTDFPMAVFKSVNNP
VTIKFTATSAQTGAATLRIGTTLSFAGGRPQATINSYTGSAPAAPTNLDS
RGVTRGAYRGLGEVYDVSIPSGTIVAGTNTITINVISGSSGDTYLSPNFI
FDCVELFQ
3D structure
PDB3njv Structural and Biochemical Studies Elucidate the Mechanism of Rhamnogalacturonan Lyase from Aspergillus aculeatus.
ChainA
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.2.2.23: rhamnogalacturonan endolyase.
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 GTR A S53 R111 S53 R111
BS02 GTR A E105 R107 D139 F151 Y205 H210 E105 R107 D139 F151 Y205 H210
BS03 GTR A R451 R455 R451 R455
BS04 RAM A G137 R451 G137 R451
BS05 CA A E347 D349 Q351 D502 E347 D349 Q351 D502
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016829 lyase activity
GO:0016837 carbon-oxygen lyase activity, acting on polysaccharides
GO:0030246 carbohydrate binding
GO:0102210 rhamnogalacturonan endolyase activity
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process
GO:0009056 catabolic process
GO:0045490 pectin catabolic process
GO:0071555 cell wall organization
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:3njv, PDBe:3njv, PDBj:3njv
PDBsum3njv
PubMed20851126
UniProtQ00019|RGLA_ASPAC Rhamnogalacturonate lyase A (Gene Name=rglA)

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