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4Q12

Crystal structure of a putative uncharacterized protein Rv3404c and likely sugar N-formyltransferase from Mycobacterium tuberculosis bound to uridine diphosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004479molecular_functionmethionyl-tRNA formyltransferase activity
A0005829cellular_componentcytosol
A0006413biological_processtranslational initiation
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
A0016742molecular_functionhydroxymethyl-, formyl- and related transferase activity
A0042803molecular_functionprotein homodimerization activity
A0071951biological_processconversion of methionyl-tRNA to N-formyl-methionyl-tRNA
B0004479molecular_functionmethionyl-tRNA formyltransferase activity
B0005829cellular_componentcytosol
B0006413biological_processtranslational initiation
B0009058biological_processbiosynthetic process
B0016740molecular_functiontransferase activity
B0016742molecular_functionhydroxymethyl-, formyl- and related transferase activity
B0042803molecular_functionprotein homodimerization activity
B0071951biological_processconversion of methionyl-tRNA to N-formyl-methionyl-tRNA
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE UDP A 301
ChainResidue
AASN10
AASN210
AHOH403
AHOH406
AHOH407
AHOH413
AHOH414
AHOH459
AHIS63
ALYS65
APHE93
AGLN95
ASER135
ATYR139
AHIS205
APHE208

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
ASER131
AGLY194
AASN198
AARG201
AHOH450
BLEU187

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
AILE73
AVAL76
AARG77
ACYS78
AGLU111
AILE112

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
ALEU7
ASER32
ACYS64

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
AGLN66
AHIS110
AGLN115
AASP117

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 306
ChainResidue
AHOH463

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE UDP B 301
ChainResidue
BASN10
BHIS63
BLYS65
BPHE93
BGLN95
BSER135
BTYR139
BHIS205
BPHE208
BASN210
BHOH405
BHOH406
BHOH407
BHOH408
BHOH412
BHOH423

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 302
ChainResidue
BILE73
BVAL76
BARG77
BCYS78
BGLU111
BILE112

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 303
ChainResidue
APHE213
BSER131
BGLY194
BASN198
BARG201

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 304
ChainResidue
BSER32
BVAL45
BCYS64

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 305
ChainResidue
BCYS64
BGLN66
BASN80
BHIS110
BILE112
BGLN115
BASP117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:28665588
ChainResidueDetails
AVAL81
BVAL81

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:28665588, ECO:0007744|PDB:5VYQ
ChainResidueDetails
AASP9
BPHE62
BLYS65
BARG90
BILE112
BLEU116
BLEU175
BARG209
APHE62
ALYS65
AARG90
AILE112
ALEU116
ALEU175
AARG209
BASP9

223532

PDB entries from 2024-08-07

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