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5UHK

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

Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue GOL A 501
ChainResidue
AASP174
ATYR219
ATHR250
ATRP278
AASN280
AGOL502

site_idAC2
Number of Residues6
Detailsbinding site for residue GOL A 502
ChainResidue
AASP285
AASN313
AGOL501
AGLY67
APHE68
ALYS98

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL C 501
ChainResidue
CGLY67
CASP174
CTYR219
CTRP278
CASN280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01353, ECO:0000305|PubMed:16533067
ChainResidueDetails
AASP175
CASP175

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:28939839, ECO:0007744|PDB:5VVT
ChainResidueDetails
AGLY67
CASP174
CASP175
CTYR219
CASP285
CASN313
ALYS98
AASP174
AASP175
ATYR219
AASP285
AASN313
CGLY67
CLYS98

site_idSWS_FT_FI3
Number of Residues2
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
CSER364

222415

PDB entries from 2024-07-10

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