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2R6E

Crystal Form B2

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003678molecular_functionDNA helicase activity
A0004386molecular_functionhelicase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006260biological_processDNA replication
A0006268biological_processDNA unwinding involved in DNA replication
A0006269biological_processDNA replication, synthesis of primer
A0016787molecular_functionhydrolase activity
A0016853molecular_functionisomerase activity
A0016887molecular_functionATP hydrolysis activity
A0042802molecular_functionidentical protein binding
A1990077cellular_componentprimosome complex
B0003677molecular_functionDNA binding
B0003678molecular_functionDNA helicase activity
B0004386molecular_functionhelicase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006260biological_processDNA replication
B0006268biological_processDNA unwinding involved in DNA replication
B0006269biological_processDNA replication, synthesis of primer
B0016787molecular_functionhydrolase activity
B0016853molecular_functionisomerase activity
B0016887molecular_functionATP hydrolysis activity
B0042802molecular_functionidentical protein binding
B1990077cellular_componentprimosome complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 500
ChainResidue
AARG211
ASER213
AVAL214
AGLY215
ALYS216
ATHR217

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 500
ChainResidue
BGLY215
BLYS216
BTHR217
BARG211
BSER213
BVAL214

Functional Information from PROSITE/UniProt
site_idPS00039
Number of Residues9
DetailsDEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. LLDEADRkI
ChainResidueDetails
ALEU139-ILE147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:12235389, ECO:0000305|PubMed:23022319
ChainResidueDetails
AGLU241
BGLU241

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000305|PubMed:23022319, ECO:0007744|PDB:4ESV
ChainResidueDetails
ASER213
BSER213
BGLY215
BLYS216
BTHR217
BALA218
BARG250
BLYS418
BGLN419
BARG420
AGLY215
ALYS216
ATHR217
AALA218
AARG250
ALYS418
AGLN419
AARG420

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:23022319
ChainResidueDetails
AGLN362
BGLN362

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:23022319, ECO:0007744|PDB:4ESV
ChainResidueDetails
AARG381
AGLU382
AGLY384
BARG381
BGLU382
BGLY384

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Gamma-phosphate sensor => ECO:0000305|PubMed:12235389
ChainResidueDetails
AGLN362
BGLN362

225158

PDB entries from 2024-09-18

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