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4IQF

Crystal Structure of Methyionyl-tRNA Formyltransferase from Bacillus anthracis

Replaces:  3RFO
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004479molecular_functionmethionyl-tRNA formyltransferase activity
A0006412biological_processtranslation
A0006413biological_processtranslational initiation
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
A0019988biological_processcharged-tRNA amino acid modification
A0071951biological_processconversion of methionyl-tRNA to N-formyl-methionyl-tRNA
B0003824molecular_functioncatalytic activity
B0004479molecular_functionmethionyl-tRNA formyltransferase activity
B0006412biological_processtranslation
B0006413biological_processtranslational initiation
B0009058biological_processbiosynthetic process
B0016740molecular_functiontransferase activity
B0019988biological_processcharged-tRNA amino acid modification
B0071951biological_processconversion of methionyl-tRNA to N-formyl-methionyl-tRNA
C0003824molecular_functioncatalytic activity
C0004479molecular_functionmethionyl-tRNA formyltransferase activity
C0006412biological_processtranslation
C0006413biological_processtranslational initiation
C0009058biological_processbiosynthetic process
C0016740molecular_functiontransferase activity
C0019988biological_processcharged-tRNA amino acid modification
C0071951biological_processconversion of methionyl-tRNA to N-formyl-methionyl-tRNA
D0003824molecular_functioncatalytic activity
D0004479molecular_functionmethionyl-tRNA formyltransferase activity
D0006412biological_processtranslation
D0006413biological_processtranslational initiation
D0009058biological_processbiosynthetic process
D0016740molecular_functiontransferase activity
D0019988biological_processcharged-tRNA amino acid modification
D0071951biological_processconversion of methionyl-tRNA to N-formyl-methionyl-tRNA
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PG5 A 401
ChainResidue
ATYR123
AMSE126
AGLU127

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 402
ChainResidue
AHOH625
AALA87
AHIS108
AALA109
APHE166
AHOH527
AHOH528

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
AARG159
AHOH549

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 401
ChainResidue
BALA87
BVAL107
BHIS108
BALA109
BPRO120
BHOH508
BHOH523
BHOH524
BHOH551

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 402
ChainResidue
BTYR123
BMSE126
BGLU127
BHOH548
BHOH622

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 401
ChainResidue
CPHE12
CALA87
CHIS108
CALA109
CPRO120
CPHE166

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL D 401
ChainResidue
DPHE12
DALA87
DHIS108
DALA109
DPRO120
DPHE166

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 402
ChainResidue
DLYS129
DGLU130
DLYS131

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 403
ChainResidue
DSER294
DSER296
DGLN297
DARG300

Functional Information from PROSITE/UniProt
site_idPS00373
Number of Residues24
DetailsGART Phosphoribosylglycinamide formyltransferase active site. GiTImYMvEkLDaGdiLtqveveI
ChainResidueDetails
AGLY133-ILE156

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00182
ChainResidueDetails
ASER110
BSER110
CSER110
DSER110

223166

PDB entries from 2024-07-31

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