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7DDX

Crystal structure of KANK1 S1179F mutant in complex wtih eIF4A1

Functional Information from GO Data
ChainGOidnamespacecontents
A0030837biological_processnegative regulation of actin filament polymerization
B0003676molecular_functionnucleic acid binding
B0003724molecular_functionRNA helicase activity
B0005524molecular_functionATP binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue SO4 A 1401
ChainResidue
ASER1094
AGLU1095
ALYS1096

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 1402
ChainResidue
AHIS1321
ALYS1322
AASP1323
AILE1324

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 1403
ChainResidue
AASP1256
AARG1254
AILE1255

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 B 301
ChainResidue
BLYS193
BGLN201
BLYS202

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 B 302
ChainResidue
BGLY79
BTHR80
BGLY81
BLYS82
BTHR83

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 B 303
ChainResidue
BARG110
BTHR158
BGLY160
BARG161
BPHE192

Functional Information from PROSITE/UniProt
site_idPS00039
Number of Residues9
DetailsDEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. VLDEADEmL
ChainResidueDetails
BVAL180-LEU188

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00541
ChainResidueDetails
BALA76

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P60842
ChainResidueDetails
BSER2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P60842
ChainResidueDetails
BSER4

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P60842
ChainResidueDetails
BLYS118
BLYS174

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P60842
ChainResidueDetails
BTHR158

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
BLYS193

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:23806337
ChainResidueDetails
BLYS238

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P60842
ChainResidueDetails
BLYS146
BLYS225

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P60842
ChainResidueDetails
BLYS238

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PDB entries from 2024-07-31

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