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1RBQ

Human GAR Tfase complex structure with 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
A0006189biological_process'de novo' IMP biosynthetic process
A0009058biological_processbiosynthetic process
B0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
B0006189biological_process'de novo' IMP biosynthetic process
B0009058biological_processbiosynthetic process
C0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
C0006189biological_process'de novo' IMP biosynthetic process
C0009058biological_processbiosynthetic process
D0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
D0006189biological_process'de novo' IMP biosynthetic process
D0009058biological_processbiosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 521
ChainResidue
ATHR10
AGLY11
ASER12
AASN13
ALYS170
AHOH523
AHOH527
AHOH555

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 522
ChainResidue
AARG168
AHOH608
AHOH610
ALYS157

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 621
ChainResidue
BTHR10
BGLY11
BSER12
BASN13
BLYS170
BHOH624
BHOH632
BHOH654

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 622
ChainResidue
BLYS157
BARG168
BHOH633
BHOH711

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 C 721
ChainResidue
CGLY11
CSER12
CASN13
CLEU14
CGLN15
CALA16
CLYS45
CHIS174
CHOH749
CHOH787

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 D 821
ChainResidue
DGLY11
DSER12
DASN13
DLEU14
DGLN15
DALA16
DLYS45
DHIS174
DHOH850
DHOH857

site_idAC7
Number of Residues25
DetailsBINDING SITE FOR RESIDUE KEU A 510
ChainResidue
AARG64
ALEU85
AMET89
AARG90
AILE91
ALEU92
AASN106
AHIS108
APRO109
AGLY117
ASER118
AVAL139
AALA140
AGLU141
AASP142
AVAL143
AASP144
AHOH530
AHOH532
AHOH537
AHOH543
AHOH562
AHOH564
AHOH574
AHOH623

site_idAC8
Number of Residues22
DetailsBINDING SITE FOR RESIDUE KEU B 610
ChainResidue
BARG64
BLEU85
BMET89
BARG90
BILE91
BLEU92
BASN106
BHIS108
BPRO109
BGLY117
BSER118
BVAL139
BALA140
BGLU141
BVAL143
BASP144
BHOH623
BHOH637
BHOH646
BHOH660
BHOH706
CHOH750

site_idAC9
Number of Residues17
DetailsBINDING SITE FOR RESIDUE KEU C 710
ChainResidue
CPRO109
CGLY117
CSER118
CVAL139
CALA140
CGLU141
CVAL143
CASP144
CHOH724
CARG64
CLEU85
CMET89
CARG90
CILE91
CLEU92
CASN106
CHIS108

site_idBC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE KEU D 810
ChainResidue
DARG64
DLEU85
DMET89
DARG90
DILE91
DLEU92
DVAL97
DASN106
DHIS108
DPRO109
DGLY117
DSER118
DVAL139
DALA140
DGLU141
DVAL143
DASP144
DHOH829

Functional Information from PROSITE/UniProt
site_idPS00373
Number of Residues24
DetailsGART Phosphoribosylglycinamide formyltransferase active site. GcTVhFVaEdVDaGqiIlqeavpV
ChainResidueDetails
AGLY133-VAL156

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P08179
ChainResidueDetails
AHIS108
BHIS108
CHIS108
DHIS108

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12450384, ECO:0000269|PubMed:16026156, ECO:0007744|PDB:1MEN, ECO:0007744|PDB:1ZLY
ChainResidueDetails
AGLY11
ALYS170
BGLY11
BLYS170
CGLY11
CLYS170
DGLY11
DLYS170

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:12755606, ECO:0007744|PDB:1NJS
ChainResidueDetails
AARG64
AASN106
BARG64
BASN106
CARG64
CASN106
DARG64
DASN106

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:12755606, ECO:0000305|PubMed:16026156, ECO:0007744|PDB:1NJS, ECO:0007744|PDB:1ZLY
ChainResidueDetails
AMET89
AALA140
BMET89
BALA140
CMET89
CALA140
DMET89
DALA140

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Raises pKa of active site His => ECO:0000250|UniProtKB:P08179
ChainResidueDetails
AASP144
BASP144
CASP144
DASP144

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
ATHR135
AASN106
AASP144
AHIS108

site_idCSA10
Number of Residues2
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
BASP144
BHIS108

site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
CASP144
CHIS108

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
DASP144
DHIS108

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
BTHR135
BASN106
BASP144
BHIS108

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
CTHR135
CASN106
CASP144
CHIS108

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
DTHR135
DASN106
DASP144
DHIS108

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
AASN106
AASP144
AHIS108

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
BASN106
BASP144
BHIS108

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
CASN106
CASP144
CHIS108

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
DASN106
DASP144
DHIS108

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
AASP144
AHIS108

226707

PDB entries from 2024-10-30

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