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2F3Q

Crystal structure of the glycogen phosphorylase B / methyl-N-(beta-D-glucopyranosyl)oxamate complex

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
A0008152biological_processmetabolic process
A0008184molecular_functionglycogen phosphorylase activity
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0098723cellular_componentskeletal muscle myofibril
A0102250molecular_functionlinear malto-oligosaccharide phosphorylase activity
A0102499molecular_functionSHG alpha-glucan phosphorylase activity
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 Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P11217
ChainResidueDetails
AARG43
AARG310

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:3616621
ChainResidueDetails
AGLU76

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Involved in the association of subunits => ECO:0000303|PubMed:728424
ChainResidueDetails
AASP109
APHE143

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424
ChainResidueDetails
AGLY156

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:3015680
ChainResidueDetails
AARG2

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217
ChainResidueDetails
AVAL15

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09812
ChainResidueDetails
AGLY204
AASP227

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3
ChainResidueDetails
ALEU430

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3
ChainResidueDetails
AGLU473

site_idSWS_FT_FI10
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09812
ChainResidueDetails
AASP514
ASER747
AGLY748

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:7500360, ECO:0000269|PubMed:8976550, ECO:0007744|PDB:2PRI, ECO:0007744|PDB:2SKC, ECO:0007744|PDB:2SKD, ECO:0007744|PDB:2SKE
ChainResidueDetails
APHE681

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 205
ChainResidueDetails
ATHR378electrostatic stabiliser
AARG569electrostatic stabiliser
AILE570electrostatic stabiliser
AARG575electrostatic stabiliser
AGLY677electrostatic stabiliser
APHE681covalently attached

217705

PDB entries from 2024-03-27

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