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5UHP

Crystal structure of the core catalytic domain of human O-GlcNAcase

Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue GOL A 501
ChainResidue
ALYS98
AASP174
ATYR219
ATHR250
AVAL254
ATRP278
AASN280

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL B 501
ChainResidue
BASP175
BTYR219
BTHR250
BTRP278
BASN280
BLYS98
BASP174

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL C 501
ChainResidue
CLYS98
CASP174
CCYS215
CTYR219
CTHR250
CTRP278
CASN280

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL D 501
ChainResidue
DLYS98
DASP174
DCYS215
DTYR219
DTHR250
DTRP278
DASN280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01353, ECO:0000305|PubMed:16533067
ChainResidueDetails
AASP175
BASP175
CASP175
DASP175

site_idSWS_FT_FI2
Number of Residues28
DetailsBINDING: BINDING => ECO:0000269|PubMed:28939839, ECO:0007744|PDB:5VVT
ChainResidueDetails
AGLY67
BASP174
BASP175
BTYR219
BASP285
BASN313
CGLY67
CLYS98
CASP174
CASP175
CTYR219
ALYS98
CASP285
CASN313
DGLY67
DLYS98
DASP174
DASP175
DTYR219
DASP285
DASN313
AASP174
AASP175
ATYR219
AASP285
AASN313
BGLY67
BLYS98

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER364
BSER364
CSER364
DSER364

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PDB entries from 2024-07-31

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