Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4A4Z

CRYSTAL STRUCTURE OF THE S. CEREVISIAE DEXH HELICASE SKI2 BOUND TO AMPPNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003723molecular_functionRNA binding
A0003724molecular_functionRNA helicase activity
A0005524molecular_functionATP binding
A0006401biological_processRNA catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ANP A 2288
ChainResidue
APHE328
ALYS357
ATHR358
AARG763
AARG767
AHOH2078
AHOH2080
AGLU329
AASP331
AGLN334
AHIS352
ATHR353
ASER354
AALA355
AGLY356

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 2289
ChainResidue
AGLU640
ALYS683
ATHR684
AVAL694
AHOH2133

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 2290
ChainResidue
ALYS636
AGLY697
ATHR722
ATHR724
AHOH2067

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 2291
ChainResidue
AALA383
ALYS704
AGLU708

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 2292
ChainResidue
ATYR1125
ALEU1127
AVAL1128
AGLU1200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues177
DetailsDomain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsMotif: {"description":"DEVH box"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon