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5IFU

Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum in complex with Glyburide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004827molecular_functionproline-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006418biological_processtRNA aminoacylation for protein translation
A0006433biological_processprolyl-tRNA aminoacylation
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004827molecular_functionproline-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006418biological_processtRNA aminoacylation for protein translation
B0006433biological_processprolyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue GBM A 801
ChainResidue
ATYR266
AILE276
AGLU404
AARG514
AGLY517
ATYR746

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 802
ChainResidue
BASP280
BILE281
AMET364
ATYR365
ASER366

site_idAC3
Number of Residues5
Detailsbinding site for residue FMT A 803
ChainResidue
ASER536
ALYS537
ATYR538
AILE595
AHOH909

site_idAC4
Number of Residues2
Detailsbinding site for residue FMT A 804
ChainResidue
ATYR278
ATHR402

site_idAC5
Number of Residues3
Detailsbinding site for residue FMT A 805
ChainResidue
ALYS445
AHOH1044
AHOH1045

site_idAC6
Number of Residues4
Detailsbinding site for residue FMT A 806
ChainResidue
ASER468
ASER655
ALYS672
ALYS673

site_idAC7
Number of Residues4
Detailsbinding site for residue FMT A 807
ChainResidue
ACYS622
AGLU632
AHOH963
AHOH1040

site_idAC8
Number of Residues3
Detailsbinding site for residue FMT A 808
ChainResidue
APRO725
AASN726
AARG738

site_idAC9
Number of Residues3
Detailsbinding site for residue FMT A 809
ChainResidue
APRO724
APRO725
AASN726

site_idAD1
Number of Residues3
Detailsbinding site for residue FMT A 810
ChainResidue
AGLU404
ATHR512
AARG514

site_idAD2
Number of Residues3
Detailsbinding site for residue FMT A 811
ChainResidue
AGLN658
AMET727
AHOH924

site_idAD3
Number of Residues2
Detailsbinding site for residue FMT A 812
ChainResidue
AASP719
AHOH952

site_idAD4
Number of Residues6
Detailsbinding site for residue EDO A 813
ChainResidue
AGLU296
AGLN299
AALA300
AASN303
AHOH966
BEDO806

site_idAD5
Number of Residues6
Detailsbinding site for residue GBM B 801
ChainResidue
BTYR266
BILE276
BGLU404
BTHR513
BARG514
BGLY517

site_idAD6
Number of Residues4
Detailsbinding site for residue FMT B 802
ChainResidue
BSER536
BLYS537
BTYR538
BHOH912

site_idAD7
Number of Residues1
Detailsbinding site for residue FMT B 803
ChainResidue
BTYR278

site_idAD8
Number of Residues5
Detailsbinding site for residue FMT B 804
ChainResidue
AGLN299
AASN303
BTYR292
BGLN299
BHOH909

site_idAD9
Number of Residues2
Detailsbinding site for residue FMT B 805
ChainResidue
BTHR512
BARG514

site_idAE1
Number of Residues5
Detailsbinding site for residue EDO B 806
ChainResidue
AEDO813
BGLU296
BGLN299
BALA300
BASN303

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|Ref.7, ECO:0007744|PDB:6T7K
ChainResidueDetails
AARG390
AHIS480
BARG390
BHIS480

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:25817387, ECO:0000269|PubMed:27798837, ECO:0000269|Ref.4, ECO:0007744|PDB:4OLF, ECO:0007744|PDB:4Q15, ECO:0007744|PDB:4YDQ
ChainResidueDetails
AARG401
AGLN475
ATHR512
BARG401
BGLN475
BTHR512

226707

PDB entries from 2024-10-30

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