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6I4M

Crystal Structure of Plasmodium berghei actin II in the Mg-ADP state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0035891biological_processexit from host cell
A0044129biological_processpositive regulation of development of symbiont in host
A0044782biological_processcilium organization
A0048232biological_processmale gamete generation
G0051015molecular_functionactin filament binding
Functional Information from PDB Data
site_idAC1
Number of Residues28
Detailsbinding site for residue ADP A 401
ChainResidue
AGLY13
ALYS213
AGLU214
AGLY302
AGLY303
ATHR304
AMET306
ATYR307
ALYS337
AMG402
AHOH551
ASER14
AHOH569
AHOH570
AHOH577
AHOH592
AHOH606
AHOH629
AHOH652
AHOH696
AHOH713
AGLY15
AMET16
ALYS18
AGLY156
AASP157
AGLY182
AARG210

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 402
ChainResidue
AADP401
AHOH506
AHOH570
AHOH577
AHOH592
AHOH696

site_idAC3
Number of Residues7
Detailsbinding site for residue SCN A 403
ChainResidue
AALA144
ASER145
APRO333
AGLU335
AHOH586
AHOH678
GGLN71

site_idAC4
Number of Residues6
Detailsbinding site for residue SCN A 404
ChainResidue
AARG62
AMET284
AARG291
ATYR295
APRO323
AHOH614

site_idAC5
Number of Residues6
Detailsbinding site for residue CA G 201
ChainResidue
AGLU167
GASP85
GGLY90
GALA92
GHOH391
GHOH393

site_idAC6
Number of Residues6
Detailsbinding site for residue CA G 202
ChainResidue
GGLY41
GASP42
GGLU73
GVAL121
GHOH373
GHOH380

Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQn.KRG
ChainResidueDetails
ATYR53-GLY63

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. LLTEApLNPktNR
ChainResidueDetails
ALEU104-ARG116

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
ALYS18
AASP157
ALYS213
AGLY303
GGLY90

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06396
ChainResidueDetails
GLEU84
AVAL159

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:31199804
ChainResidueDetails
AHIC73

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PDB entries from 2024-06-12

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