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5LBA

Crystal structure of human RECQL5 helicase in complex with DSPL fragment(1-cyclohexyl-3-(oxolan-2-ylmethyl)urea, SGC - Diamond XChem I04-1 fragment screening.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004386molecular_functionhelicase activity
A0005524molecular_functionATP binding
A0006310biological_processDNA recombination
B0003676molecular_functionnucleic acid binding
B0004386molecular_functionhelicase activity
B0005524molecular_functionATP binding
B0006310biological_processDNA recombination
C0003676molecular_functionnucleic acid binding
C0004386molecular_functionhelicase activity
C0005524molecular_functionATP binding
C0006310biological_processDNA recombination
D0003676molecular_functionnucleic acid binding
D0004386molecular_functionhelicase activity
D0005524molecular_functionATP binding
D0006310biological_processDNA recombination
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue MG B 501
ChainResidue
BADP503
BHOH607
BHOH634
BHOH646

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN B 502
ChainResidue
BCYS411
BCYS427
BCYS431
BCYS434

site_idAC3
Number of Residues18
Detailsbinding site for residue ADP B 503
ChainResidue
BSER28
BPHE29
BLYS30
BGLN34
BTHR54
BGLY55
BALA56
BGLY57
BLYS58
BSER59
BLEU60
BMG501
BHOH622
BHOH633
BHOH634
BHOH646
BHOH652
BPHE26

site_idAC4
Number of Residues4
Detailsbinding site for residue DMS B 504
ChainResidue
BILE263
BTYR265
BILE317
BPHE319

site_idAC5
Number of Residues8
Detailsbinding site for residue 6SV B 505
ChainResidue
BALA193
BTHR194
BALA195
BTYR344
BGLN345
BPHE420
BHOH630
BHOH660

site_idAC6
Number of Residues6
Detailsbinding site for residue MG A 501
ChainResidue
AASP157
AADP502
AHOH601
AHOH616
AHOH637
AHOH646

site_idAC7
Number of Residues15
Detailsbinding site for residue ADP A 502
ChainResidue
APHE26
ASER28
APHE29
ALYS30
AGLN34
ATHR54
AGLY55
AALA56
AGLY57
ALYS58
ASER59
AMG501
AHOH601
AHOH616
AHOH650

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN A 503
ChainResidue
ACYS411
ACYS427
ACYS431
ACYS434

site_idAC9
Number of Residues3
Detailsbinding site for residue DMS A 504
ChainResidue
AALA193
AALA195
APHE420

site_idAD1
Number of Residues3
Detailsbinding site for residue MG C 501
ChainResidue
CASP157
CADP503
CHOH610

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN C 502
ChainResidue
CCYS411
CCYS427
CCYS431
CCYS434

site_idAD3
Number of Residues13
Detailsbinding site for residue ADP C 503
ChainResidue
CPHE26
CSER28
CPHE29
CLYS30
CGLN34
CGLY55
CALA56
CGLY57
CLYS58
CSER59
CMG501
CHOH610
CHOH657

site_idAD4
Number of Residues4
Detailsbinding site for residue MG D 501
ChainResidue
DASP157
DADP503
DHOH621
DHOH631

site_idAD5
Number of Residues4
Detailsbinding site for residue ZN D 502
ChainResidue
DCYS411
DCYS427
DCYS431
DCYS434

site_idAD6
Number of Residues17
Detailsbinding site for residue ADP D 503
ChainResidue
DPRO53
DGLY55
DALA56
DGLY57
DLYS58
DSER59
DMG501
DHOH612
DHOH621
DHOH631
DHOH640
DHOH646
DPHE26
DSER28
DPHE29
DLYS30
DGLN34

site_idAD7
Number of Residues5
Detailsbinding site for residue DMS D 504
ChainResidue
DILE263
DTYR265
DILE317
DSER318
DPHE319

Functional Information from PROSITE/UniProt
site_idPS00690
Number of Residues10
DetailsDEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. SyLVVDEAHC
ChainResidueDetails
BSER152-CYS161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsBINDING: BINDING => ECO:0000305|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LBA
ChainResidueDetails
BPHE26
APHE26
ASER28
ALYS30
AGLN34
AGLY55
AALA56
AGLY57
ALYS58
ASER59
CPHE26
BSER28
CSER28
CLYS30
CGLN34
CGLY55
CALA56
CGLY57
CLYS58
CSER59
DPHE26
DSER28
BLYS30
DLYS30
DGLN34
DGLY55
DALA56
DGLY57
DLYS58
DSER59
BGLN34
BGLY55
BALA56
BGLY57
BLYS58
BSER59

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:5LB5
ChainResidueDetails
BPRO53
APRO53
CPRO53
DPRO53

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LB8, ECO:0007744|PDB:5LBA
ChainResidueDetails
BCYS411
DCYS411
DCYS431
DCYS434
BCYS431
BCYS434
ACYS411
ACYS431
ACYS434
CCYS411
CCYS431
CCYS434

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LBA
ChainResidueDetails
BCYS427
ACYS427
CCYS427
DCYS427

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PDB entries from 2024-07-24

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