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4UR9

Structure of ligand bound glycosylhydrolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0006517biological_processprotein deglycosylation
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0042802molecular_functionidentical protein binding
A0102571molecular_function[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity
A1901135biological_processcarbohydrate derivative metabolic process
B0005975biological_processcarbohydrate metabolic process
B0006517biological_processprotein deglycosylation
B0016231molecular_functionbeta-N-acetylglucosaminidase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0042802molecular_functionidentical protein binding
B0102571molecular_function[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity
B1901135biological_processcarbohydrate derivative metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BK9 A 1717
ChainResidue
ATYR137
AASP344
AARG347
ATYR550
AOAN1718

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BK9 B 1717
ChainResidue
BOAN1718
BTYR137
BASP344
BARG347
BTYR550

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE OAN A 1718
ChainResidue
AGLY135
APHE136
ATYR137
ALYS166
AASP242
AASP243
ATYR282
ATRP286
AVAL314
ATRP337
AASN339
AASP344
ATYR345
AASN372
ABK91717

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE OAN B 1718
ChainResidue
BGLY135
BPHE136
BTYR137
BLYS166
BASP242
BASP243
BTYR282
BTRP286
BVAL314
BASN339
BASP344
BTYR345
BASN372
BHIS433
BBK91717

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1719
ChainResidue
BGLU32
BGLU61
BASP64
BHOH2014
BHOH2015
BHOH2028

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01353, ECO:0000269|PubMed:16565725
ChainResidueDetails
AASP243
BASP243

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:16565725
ChainResidueDetails
AGLY135
BASP242
BTYR282
BTRP337
BASP344
BASN372
ALYS166
AASP242
ATYR282
ATRP337
AASP344
AASN372
BGLY135
BLYS166

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PDB entries from 2024-07-10

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