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4TTJ

Crystal structure of double mutant E. Coli purine nucleoside phosphorylase with 6 FMC molecules

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004731molecular_functionpurine-nucleoside phosphorylase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006152biological_processpurine nucleoside catabolic process
A0006974biological_processDNA damage response
A0009116biological_processnucleoside metabolic process
A0009164biological_processnucleoside catabolic process
A0016020cellular_componentmembrane
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0019686biological_processpurine nucleoside interconversion
A0042278biological_processpurine nucleoside metabolic process
A0042802molecular_functionidentical protein binding
A0047975molecular_functionguanosine phosphorylase activity
B0003824molecular_functioncatalytic activity
B0004731molecular_functionpurine-nucleoside phosphorylase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006139biological_processnucleobase-containing compound metabolic process
B0006152biological_processpurine nucleoside catabolic process
B0006974biological_processDNA damage response
B0009116biological_processnucleoside metabolic process
B0009164biological_processnucleoside catabolic process
B0016020cellular_componentmembrane
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0019686biological_processpurine nucleoside interconversion
B0042278biological_processpurine nucleoside metabolic process
B0042802molecular_functionidentical protein binding
B0047975molecular_functionguanosine phosphorylase activity
D0003824molecular_functioncatalytic activity
D0004731molecular_functionpurine-nucleoside phosphorylase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006139biological_processnucleobase-containing compound metabolic process
D0006152biological_processpurine nucleoside catabolic process
D0006974biological_processDNA damage response
D0009116biological_processnucleoside metabolic process
D0009164biological_processnucleoside catabolic process
D0016020cellular_componentmembrane
D0016757molecular_functionglycosyltransferase activity
D0016763molecular_functionpentosyltransferase activity
D0019686biological_processpurine nucleoside interconversion
D0042278biological_processpurine nucleoside metabolic process
D0042802molecular_functionidentical protein binding
D0047975molecular_functionguanosine phosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue PO4 A 301
ChainResidue
APRO19
AGLY20
AARG24
AARG87
AGLY89
ASER90
AFMC302
DARG43

site_idAC2
Number of Residues18
Detailsbinding site for residue FMC A 302
ChainResidue
AARG87
ASER90
ACYS91
AGLY92
APHE159
AVAL178
AGLU179
AMET180
AGLU181
ASER203
APO4301
AHOH537
AHOH584
AHOH634
AHOH684
DHIS4
DARG43
AMET64

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 303
ChainResidue
AASN222
AASP223
AHOH527
AHOH533
AHOH564
AHOH637

site_idAC4
Number of Residues8
Detailsbinding site for residue PO4 B 301
ChainResidue
BGLY20
BARG43
BARG87
BGLY89
BSER90
BFMC302
BHOH401
BHOH403

site_idAC5
Number of Residues17
Detailsbinding site for residue FMC B 302
ChainResidue
BHIS4
BARG43
BMET64
BARG87
BSER90
BCYS91
BGLY92
BPHE159
BVAL178
BGLU179
BMET180
BGLU181
BILE206
BPO4301
BHOH434
BHOH559
BHOH584

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 B 303
ChainResidue
BLYS99
BLEU100
BHIS205
BGLU210

site_idAC7
Number of Residues3
Detailsbinding site for residue SO4 B 304
ChainResidue
BGLN218
BTHR219
BASN222

site_idAC8
Number of Residues8
Detailsbinding site for residue PO4 D 301
ChainResidue
AARG43
DGLY20
DARG87
DGLY89
DSER90
DFMC302
DHOH461
DHOH600

site_idAC9
Number of Residues15
Detailsbinding site for residue FMC D 302
ChainResidue
AHIS4
AARG43
DMET64
DARG87
DSER90
DCYS91
DGLY92
DPHE159
DVAL178
DGLU179
DMET180
DGLU181
DPO4301
DHOH569
DHOH679

Functional Information from PROSITE/UniProt
site_idPS01232
Number of Residues16
DetailsPNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGiPScSIytkEL
ChainResidueDetails
AGLY61-LEU76

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:30337572
ChainResidueDetails
AALA204
BALA204
DALA204

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
ChainResidueDetails
AHIS4
BHIS4
DHIS4

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: in other chain => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
ChainResidueDetails
AGLY20
AARG24
AARG87
BGLY20
BARG24
BARG87
DGLY20
DARG24
DARG87

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
ChainResidueDetails
AARG43
BARG43
DARG43

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: in other chain => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
ChainResidueDetails
AGLU179
ASER203
BGLU179
BSER203
DGLU179
DSER203

site_idSWS_FT_FI6
Number of Residues3
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572
ChainResidueDetails
AALA217
BALA217
DALA217

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS26
BLYS26
DLYS26

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 375
ChainResidueDetails
AGLY20electrostatic stabiliser
AARG24electrostatic stabiliser
AARG43electrostatic stabiliser
AARG87electrostatic stabiliser
ASER90electrostatic stabiliser
AALA204proton shuttle (general acid/base)
AALA217enhance reactivity

site_idMCSA2
Number of Residues7
DetailsM-CSA 375
ChainResidueDetails
BGLY20electrostatic stabiliser
BARG24electrostatic stabiliser
BARG43electrostatic stabiliser
BARG87electrostatic stabiliser
BSER90electrostatic stabiliser
BALA204proton shuttle (general acid/base)
BALA217enhance reactivity

site_idMCSA3
Number of Residues7
DetailsM-CSA 375
ChainResidueDetails
DGLY20electrostatic stabiliser
DARG24electrostatic stabiliser
DARG43electrostatic stabiliser
DARG87electrostatic stabiliser
DSER90electrostatic stabiliser
DALA204proton shuttle (general acid/base)
DALA217enhance reactivity

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PDB entries from 2024-10-16

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