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1RMG

RHAMNOGALACTURONASE A FROM ASPERGILLUS ACULEATUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004650molecular_functionpolygalacturonase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046576molecular_functionrhamnogalacturonan alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronide lyase activity
A0071555biological_processcell wall organization
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AASP197

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AHIS272

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN32
AASN299

site_idSWS_FT_FI4
Number of Residues11
DetailsCARBOHYD: O-linked (Man) threonine
ChainResidueDetails
ATHR367
ATHR405
ATHR408
ATHR370
ATHR371
ATHR372
ATHR374
ATHR376
ATHR385
ATHR386
ATHR398

site_idSWS_FT_FI5
Number of Residues7
DetailsCARBOHYD: O-linked (Man) serine
ChainResidueDetails
ASER368
ASER373
ASER380
ASER383
ASER400
ASER409
ASER418

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PDB entries from 2024-07-24

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