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4CDG

Crystal structure of the Bloom's syndrome helicase BLM in complex with Nanobody

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003676molecular_functionnucleic acid binding
A0004386molecular_functionhelicase activity
A0005524molecular_functionATP binding
A0006260biological_processDNA replication
A0006281biological_processDNA repair
A0006310biological_processDNA recombination
A0043138molecular_function3'-5' DNA helicase activity
A0044237biological_processcellular metabolic process
B0000166molecular_functionnucleotide binding
B0003676molecular_functionnucleic acid binding
B0004386molecular_functionhelicase activity
B0005524molecular_functionATP binding
B0006260biological_processDNA replication
B0006281biological_processDNA repair
B0006310biological_processDNA recombination
B0043138molecular_function3'-5' DNA helicase activity
B0044237biological_processcellular metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ADP A 1634
ChainResidue
ALEU665
AARG982
AASN1242
AASN667
AARG669
AGLN672
AGLY692
AGLY693
AGLY694
ALYS695
ASER696

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1643
ChainResidue
ACYS1036
ACYS1055
ACYS1063
ACYS1066

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ADP B 1634
ChainResidue
BLEU665
BASN667
BARG669
BGLN672
BPRO690
BGLY692
BGLY693
BGLY694
BLYS695
BSER696
BARG982
BASN1242

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1643
ChainResidue
BCYS1036
BCYS1055
BCYS1063
BCYS1066

Functional Information from PROSITE/UniProt
site_idPS00690
Number of Residues10
DetailsDEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. ArFVIDEAHC
ChainResidueDetails
AALA790-CYS799

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:24816114, ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CDG, ECO:0007744|PDB:4CGZ, ECO:0007744|PDB:4O3M
ChainResidueDetails
APHE668
BCYS1055
BCYS1063
BCYS1066
AGLY692
ACYS1036
ACYS1055
ACYS1063
ACYS1066
BPHE668
BGLY692
BCYS1036

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CDG, ECO:0007744|PDB:4CGZ
ChainResidueDetails
AARG982
AASN1242
BARG982
BASN1242

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: 3' overhang DNA-binding => ECO:0000269|PubMed:25901030
ChainResidueDetails
AARG717
AARG808
BARG717
BARG808

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: 3' overhang DNA-binding; via amide nitrogen => ECO:0000269|PubMed:24816114, ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ, ECO:0007744|PDB:4O3M
ChainResidueDetails
AALA920
BALA920

site_idSWS_FT_FI5
Number of Residues6
DetailsSITE: 3' overhang DNA-binding => ECO:0000269|PubMed:24816114, ECO:0000269|PubMed:25901030, ECO:0007744|PDB:4CGZ, ECO:0007744|PDB:4O3M
ChainResidueDetails
ATHR946
ALYS968
ATHR1110
BTHR946
BLYS968
BTHR1110

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS863
BLYS863

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1197
BSER1197

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER1295
ASER1296
BSER1295
BSER1296

site_idSWS_FT_FI9
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS1125
ALYS1199
ALYS1207
BLYS1125
BLYS1199
BLYS1207

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PDB entries from 2024-07-17

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