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2J62

Structure of a bacterial O-glcnacase in complex with glcnacstatin

Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A1625
ChainResidue
APHE265

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A1627
ChainResidue
BPHE265

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B1626
ChainResidue
BTHR560
BLYS593

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GSZ A1626
ChainResidue
ATYR335
ATHR366
AVAL370
ATRP394
AASN396
AASP401
ATYR402
AASN429
BASP620
BLEU623
AGLY187
APHE188
ALYS218
AASP297
AASP298

site_idAC5
Number of Residues14
DetailsBINDING SITE FOR RESIDUE GSZ B1627
ChainResidue
BGLY187
BPHE188
BTYR189
BLYS218
BASP297
BASP298
BTYR335
BTHR366
BVAL370
BTRP394
BASN396
BASP401
BTYR402
BASN429

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01353, ECO:0000269|PubMed:16541109
ChainResidueDetails
AASP298
BASP298

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:16541109
ChainResidueDetails
AGLY187
AASP297
ATYR335
ATRP394
AASP401
AASN429
BGLY187
BLYS218
BASP297
BTYR335
BTRP394
BASP401
BASN429
ALYS218

219869

PDB entries from 2024-05-15

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