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6EQL

Crystal Structure of Human Glycogenin-1 (GYG1) Tyr195pIPhe mutant complexed with manganese and UDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0016757molecular_functionglycosyltransferase activity
B0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue UDP A 301
ChainResidue
ALEU9
AHIS212
ALEU214
AGLY215
ALYS218
AMN302
ATHR10
ATHR11
AASN12
ATYR15
AARG30
AASP102
AALA103
AASP104

site_idAC2
Number of Residues4
Detailsbinding site for residue MN A 302
ChainResidue
AASP102
AASP104
AHIS212
AUDP301

site_idAC3
Number of Residues16
Detailsbinding site for residue UDP B 301
ChainResidue
BLEU9
BTHR10
BTHR11
BASN12
BTYR15
BVAL82
BASP102
BALA103
BASP104
BHIS212
BLEU214
BGLY215
BLYS218
BMN302
B2PE303
BEDO304

site_idAC4
Number of Residues4
Detailsbinding site for residue MN B 302
ChainResidue
BASP102
BASP104
BHIS212
BUDP301

site_idAC5
Number of Residues10
Detailsbinding site for residue 2PE B 303
ChainResidue
BASP125
BASN133
BSER134
BGLY162
BASP163
BGLN164
BGLY215
BUDP301
BEDO304
BHOH413

site_idAC6
Number of Residues2
Detailsbinding site for residue EDO B 304
ChainResidue
BUDP301
B2PE303

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O
ChainResidueDetails
ALEU9
BLEU9

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N, ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V, ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X
ChainResidueDetails
AARG77
BARG77

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3QVB, ECO:0007744|PDB:3RMV, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N, ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2T, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V, ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X
ChainResidueDetails
AASP102
AASP104
AHIS212
BASP102
BASP104
BHIS212

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O
ChainResidueDetails
AASN133
AASP160
BASN133
BASP160

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000250|UniProtKB:P13280
ChainResidueDetails
ALYS86
BLYS86

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
ATHR2
BTHR2

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13280
ChainResidueDetails
ASER44
BSER44

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: O-linked (Glc...) tyrosine => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V
ChainResidueDetails
APHI195
BPHI195

219140

PDB entries from 2024-05-01

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