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2GJ4

Structure of rabbit muscle glycogen phosphorylase in complex with ligand

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0005977biological_processglycogen metabolic process
A0005980biological_processglycogen catabolic process
A0008184molecular_functionglycogen phosphorylase activity
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0098723cellular_componentskeletal muscle myofibril
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 941
ChainResidue
ATRP67
AGLN71
AARG193
AHOH1290
AHOH1331

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 942
ChainResidue
ATRP215
AARG351
AHOH1029
AHOH1447

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 943
ChainResidue
AGLN219
AVAL221
AALA272
AILE275
ALYS294

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 944
ChainResidue
APHE37
AHIS62

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 945
ChainResidue
ALEU549
ATYR553
AILE643
APHE644
ALEU645
AGLU646
AHOH1091
AHOH1437

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 946
ChainResidue
AGLU706
APHE708
APHE709
AARG786
AHOH1216
AHOH1595

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 947
ChainResidue
AARG519
AGLU702
AALA703
ATHR807
AHOH1080

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 948
ChainResidue
AGLN408
ALEU411
AASN412
AALA415

site_idAC9
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLR A 940
ChainResidue
ATYR90
AGLY134
ALYS568
ALYS574
ATYR648
AARG649
AVAL650
AGLY675
ATHR676
AGLY677
ALYS680
AHOH958
AHOH974
AHOH979
AHOH1001
AHOH1020
AHOH1321

site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 2TH A 949
ChainResidue
ATHR38
AVAL40
AHIS57
AARG60
ATRP67
AGLU190
ALYS191
AHOH975
AHOH1065
AHOH1102
AHOH1674

Functional Information from PROSITE/UniProt
site_idPS00102
Number of Residues13
DetailsPHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN
ChainResidueDetails
AGLU672-ASN684

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P11217","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"3616621","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Involved in the association of subunits","evidences":[{"source":"PubMed","id":"728424","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Can be labeled by an AMP analog; may be involved in allosteric regulation","evidences":[{"source":"PubMed","id":"728424","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PHK; in form phosphorylase A","evidences":[{"source":"UniProtKB","id":"P11217","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P09812","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9WUB3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9WUB3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09812","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"7500360","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8976550","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PRI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2SKC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2SKD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2SKE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1gpa
ChainResidueDetails
AARG569
ALYS568
ATHR676
ALYS574

site_idMCSA1
Number of Residues6
DetailsM-CSA 205
ChainResidueDetails
AHIS377electrostatic stabiliser
ALYS568electrostatic stabiliser
AARG569electrostatic stabiliser
ALYS574electrostatic stabiliser
ATHR676electrostatic stabiliser
ALYS680covalently attached

239803

PDB entries from 2025-08-06

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