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6RMC

Crystal structure of the DEAH-box ATPase Prp2 in complex with Spp2 and ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0005524molecular_functionATP binding
B0003676molecular_functionnucleic acid binding
B0005524molecular_functionATP binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue ADP A 1001
ChainResidue
AGLU321
AARG362
APHE558
AASP582
AMG1002
AHOH1101
AHOH1102
AHOH1109
AHOH1112
AHOH1115
ATHR322
AGLY323
ASER324
AGLY325
ALYS326
ATHR327
ATHR328
ASER358

site_idAC2
Number of Residues9
Detailsbinding site for residue MG A 1002
ChainResidue
ATHR327
AASP418
AGLU419
ASER578
AADP1001
AHOH1102
AHOH1109
AHOH1115
AHOH1118

site_idAC3
Number of Residues19
Detailsbinding site for residue ADP B 1001
ChainResidue
BLEU297
BGLU321
BTHR322
BGLY323
BSER324
BGLY325
BLYS326
BTHR327
BTHR328
BSER358
BARG362
BPHE558
BASP582
BARG628
BMG1002
BHOH1109
BHOH1110
BHOH1115
BHOH1116

site_idAC4
Number of Residues7
Detailsbinding site for residue MG B 1002
ChainResidue
BTHR327
BSER578
BADP1001
BHOH1110
BHOH1114
BHOH1115
BHOH1119

Functional Information from PROSITE/UniProt
site_idPS00690
Number of Residues10
DetailsDEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. ScIMIDEAHE
ChainResidueDetails
ASER413-GLU422

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PDB entries from 2024-06-12

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