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1LL2

Crystal Structure of Rabbit Muscle Glycogenin Complexed with UDP-glucose and Manganese

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005978biological_processglycogen biosynthetic process
A0008466molecular_functionglycogenin glucosyltransferase activity
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0030145molecular_functionmanganese ion binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 333
ChainResidue
AASP102
AASP104
AHIS212
AUPG334

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE UPG A 334
ChainResidue
AASP102
AALA103
AASP104
AASP125
AASN133
ASER134
AGLN164
AHIS212
ALEU214
AGLY215
ALYS218
AMN333
AHOH356
AHOH375
AHOH416
AHOH459
AHOH492
AHOH493
AHOH520
AHOH582
ALEU9
ATHR10
ATHR11
AASN12
ATYR15

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051921, ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF, ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91
ChainResidueDetails
ALEU9
ATHR11
ATYR15
AASP102
AALA103
AASP104
AASN133
AGLN164
ALYS218

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051921, ECO:0000269|PubMed:15849187, ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDG
ChainResidueDetails
AASN12

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P46976
ChainResidueDetails
AARG77
ALYS86
AASP160
AASP163

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22226635, ECO:0007744|PDB:3V91
ChainResidueDetails
ASER134

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15849187, ECO:0007744|PDB:1ZCT
ChainResidueDetails
AHIS212

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051921, ECO:0000269|PubMed:22226635, ECO:0007744|PDB:1LL2, ECO:0007744|PDB:3V91
ChainResidueDetails
AGLY215

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000269|PubMed:10049511
ChainResidueDetails
ALYS86

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N-acetylthreonine => ECO:0000250|UniProtKB:P46976
ChainResidueDetails
ATHR2

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA; in vitro => ECO:0000269|PubMed:3151442
ChainResidueDetails
ASER44

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: O-linked (Glc...) tyrosine => ECO:0000269|PubMed:8143846
ChainResidueDetails
ATYR195

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ga8
ChainResidueDetails
AGLN164
AASN133
AASP125

237735

PDB entries from 2025-06-18

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