Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3QB0

Crystal structure of Actin-related protein Arp4 from S. cerevisiae complexed with ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0000812cellular_componentSwr1 complex
A0003682molecular_functionchromatin binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0006281biological_processDNA repair
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0006351biological_processDNA-templated transcription
A0006355biological_processregulation of DNA-templated transcription
A0006357biological_processregulation of transcription by RNA polymerase II
A0016514cellular_componentSWI/SNF complex
A0031011cellular_componentIno80 complex
A0035267cellular_componentNuA4 histone acetyltransferase complex
A0042393molecular_functionhistone binding
A0043232cellular_componentintracellular non-membrane-bounded organelle
A0051382biological_processkinetochore assembly
B0000785cellular_componentchromatin
B0000812cellular_componentSwr1 complex
B0003682molecular_functionchromatin binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0006281biological_processDNA repair
B0006325biological_processchromatin organization
B0006338biological_processchromatin remodeling
B0006351biological_processDNA-templated transcription
B0006355biological_processregulation of DNA-templated transcription
B0006357biological_processregulation of transcription by RNA polymerase II
B0016514cellular_componentSWI/SNF complex
B0031011cellular_componentIno80 complex
B0035267cellular_componentNuA4 histone acetyltransferase complex
B0042393molecular_functionhistone binding
B0043232cellular_componentintracellular non-membrane-bounded organelle
B0051382biological_processkinetochore assembly
C0000785cellular_componentchromatin
C0000812cellular_componentSwr1 complex
C0003682molecular_functionchromatin binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0006281biological_processDNA repair
C0006325biological_processchromatin organization
C0006338biological_processchromatin remodeling
C0006351biological_processDNA-templated transcription
C0006355biological_processregulation of DNA-templated transcription
C0006357biological_processregulation of transcription by RNA polymerase II
C0016514cellular_componentSWI/SNF complex
C0031011cellular_componentIno80 complex
C0035267cellular_componentNuA4 histone acetyltransferase complex
C0042393molecular_functionhistone binding
C0043232cellular_componentintracellular non-membrane-bounded organelle
C0051382biological_processkinetochore assembly
D0000785cellular_componentchromatin
D0000812cellular_componentSwr1 complex
D0003682molecular_functionchromatin binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0006281biological_processDNA repair
D0006325biological_processchromatin organization
D0006338biological_processchromatin remodeling
D0006351biological_processDNA-templated transcription
D0006355biological_processregulation of DNA-templated transcription
D0006357biological_processregulation of transcription by RNA polymerase II
D0016514cellular_componentSWI/SNF complex
D0031011cellular_componentIno80 complex
D0035267cellular_componentNuA4 histone acetyltransferase complex
D0042393molecular_functionhistone binding
D0043232cellular_componentintracellular non-membrane-bounded organelle
D0051382biological_processkinetochore assembly
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ATP A 490
ChainResidue
AGLY22
AGLY412
AGLY413
ATHR414
AILE417
AGLN449
ACA491
ASER23
ATYR24
ATHR25
AGLY161
AHIS162
AASP163
AGLN240
ALYS243

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ATP B 490
ChainResidue
BGLY22
BSER23
BTYR24
BTHR25
BGLY161
BHIS162
BASP163
BGLN240
BLYS243
BGLY412
BGLY413
BTHR414
BGLN449
BCA491

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ATP C 490
ChainResidue
CGLY22
CSER23
CTYR24
CTHR25
CGLY161
CHIS162
CASP163
CGLN240
CLYS243
CGLY412
CGLY413
CTHR414
CSER416
CGLN449
CCA491

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ATP D 490
ChainResidue
DGLY22
DSER23
DTYR24
DTHR25
DGLY161
DHIS162
DASP163
DGLN240
DLYS243
DGLY412
DGLY413
DTHR414
DILE417
DGLN449
DCA491

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 491
ChainResidue
AASP159
AATP490

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA D 491
ChainResidue
DASP159
DATP490

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA C 491
ChainResidue
CATP490

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA B 491
ChainResidue
BASP159
BATP490

Functional Information from PROSITE/UniProt
site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEPvWNSteNR
ChainResidueDetails
ALEU109-ARG121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER349
BSER349
CSER349
DSER349

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon