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1RBZ

Human GAR Tfase complex structure with polyglutamated 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
Functional Information from PDB Data
site_idAC1
Number of Residues39
DetailsBINDING SITE FOR RESIDUE KT5 A 510
ChainResidue
ATHR10
AILE91
ALEU92
AVAL97
AASN106
AHIS108
APRO109
AGLY117
ASER118
AVAL139
AALA140
AGLY11
AGLU141
AVAL143
AASP144
ALYS170
AGLU173
AHOH513
AHOH516
AHOH517
AHOH519
AHOH536
ASER12
AHOH544
AHOH551
AHOH555
AHOH559
AHOH563
AHOH565
AHOH577
BLYS45
BGLU167
BHOH665
ALYS37
AARG64
ALEU85
AGLY87
AMET89
AARG90

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE KT5 B 610
ChainResidue
BARG64
BMET89
BARG90
BILE91
BLEU92
BVAL97
BASN106
BHIS108
BPRO109
BGLY117
BSER118
BVAL139
BALA140
BGLU141
BVAL143
BASP144
BHOH616
BHOH677

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 Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P08179
ChainResidueDetails
AHIS108
BHIS108

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12450384, ECO:0000269|PubMed:16026156, ECO:0007744|PDB:1MEN, ECO:0007744|PDB:1ZLY
ChainResidueDetails
AGLY11
ALYS170
BGLY11
BLYS170

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:12755606, ECO:0007744|PDB:1NJS
ChainResidueDetails
AARG64
AASN106
BARG64
BASN106

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:12755606, ECO:0000305|PubMed:16026156, ECO:0007744|PDB:1NJS, ECO:0007744|PDB:1ZLY
ChainResidueDetails
AMET89
AALA140
BMET89
BALA140

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Raises pKa of active site His => ECO:0000250|UniProtKB:P08179
ChainResidueDetails
AASP144
BASP144

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

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

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
AASN106
AASP144
AHIS108

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
BASN106
BASP144
BHIS108

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
AASP144
AHIS108

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
BASP144
BHIS108

224572

PDB entries from 2024-09-04

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