Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4JHD

Crystal Structure of an Actin Dimer in Complex with the Actin Nucleator Cordon-Bleu

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000281biological_processmitotic cytokinesis
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005856cellular_componentcytoskeleton
A0006338biological_processchromatin remodeling
A0007010biological_processcytoskeleton organization
A0007291biological_processsperm individualization
A0015629cellular_componentactin cytoskeleton
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0030723biological_processovarian fusome organization
A0031011cellular_componentIno80 complex
A0032507biological_processmaintenance of protein location in cell
A0035060cellular_componentbrahma complex
A0035148biological_processtube formation
A0048468biological_processcell development
A0048646biological_processanatomical structure formation involved in morphogenesis
B0000166molecular_functionnucleotide binding
B0000281biological_processmitotic cytokinesis
B0005200molecular_functionstructural constituent of cytoskeleton
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005856cellular_componentcytoskeleton
B0006338biological_processchromatin remodeling
B0007010biological_processcytoskeleton organization
B0007291biological_processsperm individualization
B0015629cellular_componentactin cytoskeleton
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0030723biological_processovarian fusome organization
B0031011cellular_componentIno80 complex
B0032507biological_processmaintenance of protein location in cell
B0035060cellular_componentbrahma complex
B0035148biological_processtube formation
B0048468biological_processcell development
B0048646biological_processanatomical structure formation involved in morphogenesis
C0003779molecular_functionactin binding
C0003785molecular_functionactin monomer binding
D0000166molecular_functionnucleotide binding
D0000281biological_processmitotic cytokinesis
D0005200molecular_functionstructural constituent of cytoskeleton
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005856cellular_componentcytoskeleton
D0006338biological_processchromatin remodeling
D0007010biological_processcytoskeleton organization
D0007291biological_processsperm individualization
D0015629cellular_componentactin cytoskeleton
D0016787molecular_functionhydrolase activity
D0016887molecular_functionATP hydrolysis activity
D0030723biological_processovarian fusome organization
D0031011cellular_componentIno80 complex
D0032507biological_processmaintenance of protein location in cell
D0035060cellular_componentbrahma complex
D0035148biological_processtube formation
D0048468biological_processcell development
D0048646biological_processanatomical structure formation involved in morphogenesis
E0000166molecular_functionnucleotide binding
E0000281biological_processmitotic cytokinesis
E0005200molecular_functionstructural constituent of cytoskeleton
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005856cellular_componentcytoskeleton
E0006338biological_processchromatin remodeling
E0007010biological_processcytoskeleton organization
E0007291biological_processsperm individualization
E0015629cellular_componentactin cytoskeleton
E0016787molecular_functionhydrolase activity
E0016887molecular_functionATP hydrolysis activity
E0030723biological_processovarian fusome organization
E0031011cellular_componentIno80 complex
E0032507biological_processmaintenance of protein location in cell
E0035060cellular_componentbrahma complex
E0035148biological_processtube formation
E0048468biological_processcell development
E0048646biological_processanatomical structure formation involved in morphogenesis
F0003779molecular_functionactin binding
F0003785molecular_functionactin monomer binding
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ANP A 401
ChainResidue
AGLY13
AGLY182
AARG210
ALYS213
AGLU214
AGLY302
ATHR303
AMET305
ATYR306
AMG402
CTYR101
ASER14
AGLY15
AMET16
ALYS18
AGLY156
AASP157
AGLY158
AVAL159

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AANP401

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ANP B 401
ChainResidue
BGLY13
BSER14
BGLY15
BMET16
BLYS18
BGLY156
BASP157
BGLY158
BGLY182
BLYS213
BGLU214
BGLY301
BGLY302
BTHR303
BMET305
BTYR306
BLYS336
BMG402
BHOH502
BHOH508
BHOH521
CALA145

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 402
ChainResidue
BANP401
BHOH502

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ANP D 401
ChainResidue
DGLY13
DSER14
DGLY15
DMET16
DLYS18
DGLY156
DASP157
DGLY158
DGLY182
DARG210
DLYS213
DGLU214
DGLY302
DTHR303
DMET305
DTYR306
DMG402
DHOH518
DHOH528
FTYR101

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG D 402
ChainResidue
DANP401
DHOH528

site_idAC7
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ANP E 401
ChainResidue
EGLY13
ESER14
EGLY15
EMET16
ELYS18
EGLY156
EASP157
EGLY158
EGLY182
ELYS213
EGLU214
EGLY302
ETHR303
EMET305
ETYR306
ELYS336
EMG402

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG E 402
ChainResidue
EANP401
EHOH502

Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR53-GLY63
BTYR53-GLY63

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WISKqEYDE
ChainResidueDetails
ATRP356-GLU364
BTRP356-GLU364

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
ALEU104-ARG116
BLEU104-ARG116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsModified residue: {"description":"Methionine sulfoxide","evidences":[{"source":"PubMed","id":"22116028","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"UniProtKB","id":"P02572","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsDomain: {"description":"WH2 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00406","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues40
DetailsDomain: {"description":"WH2 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00406","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues58
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues34
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

PDB statisticsPDBj update infoContact PDBjnumon