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1ABB

CONTROL OF PHOSPHORYLASE B CONFORMATION BY A MODIFIED COFACTOR: CRYSTALLOGRAPHIC STUDIES ON R-STATE GLYCOGEN PHOSPHORYLASE RECONSTITUTED WITH PYRIDOXAL 5'-DIPHOSPHATE

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
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
B0005737cellular_componentcytoplasm
B0005975biological_processcarbohydrate metabolic process
B0005977biological_processglycogen metabolic process
B0005980biological_processglycogen catabolic process
B0008184molecular_functionglycogen phosphorylase activity
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0030170molecular_functionpyridoxal phosphate binding
B0098723cellular_componentskeletal muscle myofibril
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
C0005737cellular_componentcytoplasm
C0005975biological_processcarbohydrate metabolic process
C0005977biological_processglycogen metabolic process
C0005980biological_processglycogen catabolic process
C0008184molecular_functionglycogen phosphorylase activity
C0016740molecular_functiontransferase activity
C0016757molecular_functionglycosyltransferase activity
C0030170molecular_functionpyridoxal phosphate binding
C0098723cellular_componentskeletal muscle myofibril
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic activity
D0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
D0005737cellular_componentcytoplasm
D0005975biological_processcarbohydrate metabolic process
D0005977biological_processglycogen metabolic process
D0005980biological_processglycogen catabolic process
D0008184molecular_functionglycogen phosphorylase activity
D0016740molecular_functiontransferase activity
D0016757molecular_functionglycosyltransferase activity
D0030170molecular_functionpyridoxal phosphate binding
D0098723cellular_componentskeletal muscle myofibril
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 900
ChainResidue
ALYS11
ASER14
AARG16
AARG69
BARG43

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 900
ChainResidue
BARG69
AARG43
BLYS11
BSER14
BARG16

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 900
ChainResidue
CLYS11
CSER14
CARG16
CARG69
DARG43

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 900
ChainResidue
CARG43
DLYS11
DSER14
DARG16
DARG69

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PDP A 931
ChainResidue
AARG138
ATRP491
ALYS568
AARG569
ALYS574
AARG649
AVAL650
ATHR676
AGLY677
ALYS680

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE IMP A 920
ChainResidue
ATRP67
AGLN71
ATYR75
AARG309
AARG310
ALYS315
BASP42
BASN44
BVAL45

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PDP B 932
ChainResidue
BTYR90
BARG138
BTRP491
BLYS568
BARG569
BLYS574
BARG649
BVAL650
BALA653
BTHR676
BGLY677
BLYS680

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE IMP B 920
ChainResidue
AASP42
AASN44
AVAL45
BTRP67
BTYR75
BGLU76
BARG309
BARG310
BLYS315

site_idAC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PDP C 933
ChainResidue
CTRP491
CLYS568
CARG569
CLYS574
CTYR648
CARG649
CVAL650
CALA653
CTHR676
CGLY677
CLYS680

site_idBC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE IMP C 920
ChainResidue
CGLN71
CTYR75
CGLU76
CTYR155
CARG309
CARG310
CLYS315
DASP42
DASN44
DVAL45

site_idBC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PDP D 934
ChainResidue
DTYR90
DARG138
DTRP491
DLYS568
DARG569
DLYS574
DVAL650
DTHR676
DGLY677
DLYS680

site_idBC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE IMP D 920
ChainResidue
DGLU76
DARG309
DARG310
DLYS315
CASP42
CASN44
CVAL45
DTRP67
DILE68
DGLN71
DGLN72
DTYR75

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 Residues40
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P11217","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"3616621","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsSite: {"description":"Involved in the association of subunits","evidences":[{"source":"PubMed","id":"728424","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
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 Residues4
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 Residues8
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P09812","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9WUB3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9WUB3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues12
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09812","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
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_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1gpa
ChainResidueDetails
BARG569
BLYS568
BTHR676
BLYS574

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1gpa
ChainResidueDetails
CARG569
CLYS568
CTHR676
CLYS574

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1gpa
ChainResidueDetails
DARG569
DLYS568
DTHR676
DLYS574

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

site_idMCSA2
Number of Residues6
DetailsM-CSA 205
ChainResidueDetails
BHIS377electrostatic stabiliser
BLYS568electrostatic stabiliser
BARG569electrostatic stabiliser
BLYS574electrostatic stabiliser
BTHR676electrostatic stabiliser
BLYS680covalently attached

site_idMCSA3
Number of Residues6
DetailsM-CSA 205
ChainResidueDetails
CHIS377electrostatic stabiliser
CLYS568electrostatic stabiliser
CARG569electrostatic stabiliser
CLYS574electrostatic stabiliser
CTHR676electrostatic stabiliser
CLYS680covalently attached

site_idMCSA4
Number of Residues6
DetailsM-CSA 205
ChainResidueDetails
DHIS377electrostatic stabiliser
DLYS568electrostatic stabiliser
DARG569electrostatic stabiliser
DLYS574electrostatic stabiliser
DTHR676electrostatic stabiliser
DLYS680covalently attached

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PDB entries from 2025-10-15

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