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1NJS

human GAR Tfase in complex with hydrolyzed form of 10-trifluoroacetyl-5,10-dideaza-acyclic-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 Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 521
ChainResidue
ATHR10
AGLY11
ASER12
AASN13
ALYS170
AHOH527
AHOH535
AHOH577

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 522
ChainResidue
AARG168
AHOH560
AHOH611
ALYS157

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PO4 B 621
ChainResidue
BGLY11
BSER12
BASN13
BLEU14
BGLN15
BALA16
BLYS45
BHIS174
BHOH652
BHOH656
BHOH705

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE KEU A 510
ChainResidue
AARG64
ALEU85
AMET89
AARG90
AILE91
ALEU92
AVAL97
AASN106
AHIS108
APRO109
AGLY117
ASER118
AVAL139
AALA140
AGLU141
AVAL143
AASP144
AHOH528
AHOH529
AHOH533
AHOH543
AHOH563
AHOH565
BHOH661

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE KEU B 610
ChainResidue
BARG64
BMET89
BARG90
BILE91
BLEU92
BVAL97
BASN106
BHIS108
BPRO109
BGLY117
BVAL139
BALA140
BGLU141
BVAL143
BASP144
BHOH631
BHOH684

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

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PDB entries from 2024-07-10

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