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

2Q8K

The crystal structure of Ebp1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003714molecular_functiontranscription corepressor activity
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0006364biological_processrRNA processing
A0006417biological_processregulation of translation
A0016020cellular_componentmembrane
A0031625molecular_functionubiquitin protein ligase binding
A0035578cellular_componentazurophil granule lumen
A0043066biological_processnegative regulation of apoptotic process
A0045597biological_processpositive regulation of cell differentiation
A0045892biological_processnegative regulation of DNA-templated transcription
A0070062cellular_componentextracellular exosome
A1990904cellular_componentribonucleoprotein complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AARG33
APRO337
AHOH815
AHOH847
AHOH877
AHOH959

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AHOH623
AHOH678
AHOH799
AHOH806
AHOH815
AHOH890
AHIS147
AARG332
AGLY336

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
ALYS191
AVAL194
AGLY197
AGLU198
AHOH729

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 504
ChainResidue
AASN171
AHIS175
AHOH684
AHOH754
AHOH767
AHOH811
AHOH1017

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 505
ChainResidue
ALYS258
AMET259
ALYS260
AHOH684
AHOH743
AHOH902

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 601
ChainResidue
AILE80
ASER81
AVAL82
APHE89
ATYR98
ATYR309

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 602
ChainResidue
APHE64
ALYS65
ALYS66
AGLU67

Functional Information from PROSITE/UniProt
site_idPS01202
Number of Residues17
DetailsMAP_2 Methionine aminopeptidase subfamily 2 signature. DLvKIDlGvHVDGfiaN
ChainResidueDetails
AASP104-ASN120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER335

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC/PRKCD => ECO:0000269|PubMed:16832058, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER361

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000305|PubMed:11325528
ChainResidueDetails
ATHR366

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
ATHR386

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS298

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xgm
ChainResidueDetails
AASP227

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon