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7ZMQ

Crystal structure of human RECQL5 helicase APO form in complex with engineered nanobody (Gluebody) G2*-006

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
Functional Information from PROSITE/UniProt
site_idPS00690
Number of Residues10
DetailsDEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. SyLVVDEAHC
ChainResidueDetails
ASER152-CYS161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000305|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LBA
ChainResidueDetails
ALYS30
AGLN34
AGLY55
AALA56
AGLY57
ALYS58
ASER59
BPHE26
BSER28
BLYS30
BGLN34
BGLY55
BALA56
BGLY57
BLYS58
BSER59
APHE26
ASER28

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:5LB5
ChainResidueDetails
APRO53
BPRO53

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LB8, ECO:0007744|PDB:5LBA
ChainResidueDetails
ACYS411
ACYS431
ACYS434
BCYS411
BCYS431
BCYS434

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LBA
ChainResidueDetails
ACYS427
BCYS427

221051

PDB entries from 2024-06-12

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