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1MDU

Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1 (GS-1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0051015molecular_functionactin filament binding
B0000166molecular_functionnucleotide binding
B0001725cellular_componentstress fiber
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005856cellular_componentcytoskeleton
B0005865cellular_componentstriated muscle thin filament
B0005884cellular_componentactin filament
B0015629cellular_componentactin cytoskeleton
B0016787molecular_functionhydrolase activity
B0030240biological_processskeletal muscle thin filament assembly
B0048741biological_processskeletal muscle fiber development
D0051015molecular_functionactin filament binding
E0000166molecular_functionnucleotide binding
E0001725cellular_componentstress fiber
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005856cellular_componentcytoskeleton
E0005865cellular_componentstriated muscle thin filament
E0005884cellular_componentactin filament
E0015629cellular_componentactin cytoskeleton
E0016787molecular_functionhydrolase activity
E0030240biological_processskeletal muscle thin filament assembly
E0048741biological_processskeletal muscle fiber development
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
BATP400
BHOH405
BHOH406
BHOH407
BHOH408
BHOH409

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AVAL121
AHOH513
AGLY41
AASP42
AGLU73

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AASP85
AGLY90
AALA92
AHOH486
AHOH505
BGLU169
BHOH413

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 404
ChainResidue
BSER325
BHOH471
BHOH472
BHOH531
BHOH572
DGLU14

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA E 401
ChainResidue
EATP400
EHOH408
EHOH410
EHOH411
EHOH480

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 402
ChainResidue
DGLY41
DASP42
DGLU73
DVAL121
DHOH418
DHOH455

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 403
ChainResidue
DASP85
DGLY90
DALA92
DHOH425
EGLU169
EHOH403

site_idAC8
Number of Residues27
DetailsBINDING SITE FOR RESIDUE ATP B 400
ChainResidue
BGLY15
BSER16
BGLY17
BLEU18
BLYS20
BGLY158
BASP159
BGLY160
BVAL161
BARG212
BLYS215
BGLU216
BGLY303
BGLY304
BTHR305
BMET307
BTYR308
BLYS338
BCA401
BHOH408
BHOH409
BHOH410
BHOH411
BHOH412
BHOH478
BHOH507
BHOH551

site_idAC9
Number of Residues24
DetailsBINDING SITE FOR RESIDUE ATP E 400
ChainResidue
EGLY15
ESER16
EGLY17
ELEU18
ELYS20
EGLY158
EASP159
EGLY160
EVAL161
EGLY184
ELYS215
EGLU216
EGLY303
EGLY304
ETHR305
EMET307
ETYR308
ELYS338
ECA401
EHOH408
EHOH410
EHOH412
EHOH433
EHOH484

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TRS A 472
ChainResidue
ATYR35
ATYR109
APHE110
ALYS111
ASER112
EASN227
EHOH454

Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
BTYR55-GLY65

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
BTRP358-GLU366

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
BLEU106-ARG118

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues164
DetailsRepeat: {"description":"Gelsolin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues123
DetailsRegion: {"description":"Actin-severing","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsRegion: {"description":"Actin-actin interfilament contact point"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19666512","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FFK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues14
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by SRC; in vitro","evidences":[{"source":"PubMed","id":"10210201","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"12356759","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MDU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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