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6I4I

Crystal Structure of Plasmodium falciparum actin I (F54Y mutant) in the Mg-K-ADP-AlFn state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005884cellular_componentactin filament
A0007010biological_processcytoskeleton organization
A0009665biological_processplastid inheritance
A0015629cellular_componentactin cytoskeleton
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0020014biological_processschizogony
A0070360biological_processactin polymerization-dependent cell-to-cell migration in host
A0085017biological_processentry into host cell by a symbiont-containing vacuole
G0051015molecular_functionactin filament binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue ADP A 401
ChainResidue
AGLY14
ALYS214
AGLU215
AGLY302
AGLY303
ATHR304
AMET306
ATYR307
ALYS337
AAF3402
AMG403
ASER15
AHOH522
AHOH535
AHOH553
AHOH570
AGLY16
AASN17
ALYS19
AGLY157
AASP158
AGLY183
AARG211

site_idAC2
Number of Residues13
Detailsbinding site for residue AF3 A 402
ChainResidue
ASER15
AGLY75
AGLY157
AASP158
AGLY159
AVAL160
AADP401
AMG403
AK404
AHOH518
AHOH570
AHOH643
AHOH658

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 403
ChainResidue
AADP401
AAF3402
AHOH518
AHOH524
AHOH570
AHOH643

site_idAC4
Number of Residues5
Detailsbinding site for residue K A 404
ChainResidue
AASP155
AGLY157
AVAL160
AAF3402
AHOH552

site_idAC5
Number of Residues1
Detailsbinding site for residue SCN A 405
ChainResidue
AGLU308

site_idAC6
Number of Residues4
Detailsbinding site for residue K A 406
ChainResidue
ATHR319
ATHR320
AALA322
ASER324

site_idAC7
Number of Residues6
Detailsbinding site for residue CA G 201
ChainResidue
GGLY41
GASP42
GGLU73
GVAL121
GHOH353
GHOH359

site_idAC8
Number of Residues6
Detailsbinding site for residue CA G 202
ChainResidue
AGLU168
AHOH630
GASP85
GGLY90
GALA92
GHOH313

Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQt.KRG
ChainResidueDetails
ATYR54-GLY64

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKeEYDE
ChainResidueDetails
ATRP357-GLU365

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkgNR
ChainResidueDetails
ALEU105-ARG117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:24743229, ECO:0000269|PubMed:28695858, ECO:0000269|PubMed:31199804, ECO:0007744|PDB:4CBU, ECO:0007744|PDB:4CBW, ECO:0007744|PDB:4CBX, ECO:0007744|PDB:5MVV, ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E, ECO:0007744|PDB:6I4F, ECO:0007744|PDB:6I4G, ECO:0007744|PDB:6I4H, ECO:0007744|PDB:6I4I, ECO:0007744|PDB:6I4J, ECO:0007744|PDB:6I4K, ECO:0007744|PDB:6I4L, ECO:0007744|PDB:6I4M
ChainResidueDetails
GARG91
GALA122
ALYS214
AGLY303
GGLY90

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06396
ChainResidueDetails
GLEU84

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:24743229, ECO:0000269|PubMed:28695858, ECO:0000269|PubMed:28923924, ECO:0000269|PubMed:31199804, ECO:0000269|PubMed:33767187, ECO:0000269|Ref.7, ECO:0007744|PDB:4CBU, ECO:0007744|PDB:5MVV, ECO:0007744|PDB:5OGW, ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E, ECO:0007744|PDB:6TU4, ECO:0007744|PDB:7ALN
ChainResidueDetails
ALYS19

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:24743229, ECO:0000269|PubMed:28695858, ECO:0000269|PubMed:31199804, ECO:0007744|PDB:4CBU, ECO:0007744|PDB:5MVV, ECO:0007744|PDB:6I4D
ChainResidueDetails
AGLY159

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:24743229, ECO:0000269|PubMed:28695858, ECO:0000269|PubMed:28923924, ECO:0000269|PubMed:31199804, ECO:0007744|PDB:4CBU, ECO:0007744|PDB:5MVV, ECO:0007744|PDB:5OGW, ECO:0007744|PDB:6I4D
ChainResidueDetails
AVAL160

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:24743229, ECO:0000269|PubMed:28695858, ECO:0000269|PubMed:31199804, ECO:0007744|PDB:4CBU, ECO:0007744|PDB:5MVV, ECO:0007744|PDB:6I4D, ECO:0007744|PDB:6I4E
ChainResidueDetails
AGLU215

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Not methylated => ECO:0000269|PubMed:31199804
ChainResidueDetails
AHIS74

221051

PDB entries from 2024-06-12

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