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3DA8

Crystal structure of PurN from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
A0046653biological_processtetrahydrofolate metabolic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006189biological_process'de novo' IMP biosynthetic process
B0009058biological_processbiosynthetic process
B0016740molecular_functiontransferase activity
B0046653biological_processtetrahydrofolate metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
AASN116
ATHR117
AHOH618
AHOH664
AHOH677
AHOH711

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 603
ChainResidue
ALEU26

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 606
ChainResidue
AGLU177

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IOD A 609
ChainResidue
AHOH739
BPHE125
BHOH759
AGLY215

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 611
ChainResidue
AHOH814

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BME A 612
ChainResidue
AALA124
APHE125
AVAL141
AHOH625
AHOH629
BLEU121
BLEU122
BALA124

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD B 610
ChainResidue
BARG51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01930
ChainResidueDetails
AHIS118
BHIS118

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01930
ChainResidueDetails
AARG74
BARG74

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AARG100
AASN116
ATHR117
AASP150
BARG100
BASN116
BTHR117
BASP150

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Raises pKa of active site His => ECO:0000255|HAMAP-Rule:MF_01930
ChainResidueDetails
AASP154
BASP154

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
AHIS118
ATHR145
AASP154
AASN116

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
BHIS118
BTHR145
BASP154
BASN116

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
AHIS118
AASP154
AASN116

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
BHIS118
BASP154
BASN116

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
AHIS118
AASP154

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1c2t
ChainResidueDetails
BHIS118
BASP154

237735

PDB entries from 2025-06-18

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