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4GLJ

Crystal structure of methylthioadenosine phosphorylase in complex with rhodamine B

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0006166biological_processpurine ribonucleoside salvage
A0009116biological_processnucleoside metabolic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
A0019509biological_processL-methionine salvage from methylthioadenosine
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE RHB A 301
ChainResidue
ASER22
AVAL278
ARHB302
APO4303
ACL305
AHOH435
AHOH574
ATYR25
AHIS65
APRO73
APHE179
AILE239
ALEU242
AMET243
AGLN275

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE RHB A 302
ChainResidue
AALA98
AGLY100
APHE179
AILE196
AGLY197
AMET198
ATHR221
AASP222
APHE223
AASP224
ACYS225
AASN229
AALA238
ARHB301
ACL304
AHOH482
AHOH575
AHOH576
AHOH579

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 A 303
ChainResidue
AGLY21
ASER22
AARG64
AHIS65
ASER97
AALA98
ATHR199
ARHB301
AHOH457
AHOH482

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 304
ChainResidue
AASP222
AASN229
ASER234
ARHB302

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 305
ChainResidue
ARHB301

Functional Information from PROSITE/UniProt
site_idPS01240
Number of Residues41
DetailsPNP_MTAP_2 Purine and other phosphorylases family 2 signature. LtrhGqgHrLtpseVpyrAn.IyAlktlGvry.IVsvSAvGSL
ChainResidueDetails
ALEU62-LEU102

223790

PDB entries from 2024-08-14

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