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4A64

Crystal structure of the N-terminal domain of human Cul4B at 2.57A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0006511biological_processubiquitin-dependent protein catabolic process
A0031625molecular_functionubiquitin protein ligase binding
B0006511biological_processubiquitin-dependent protein catabolic process
B0031625molecular_functionubiquitin protein ligase binding
C0006511biological_processubiquitin-dependent protein catabolic process
C0031625molecular_functionubiquitin protein ligase binding
D0006511biological_processubiquitin-dependent protein catabolic process
D0031625molecular_functionubiquitin protein ligase binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1534
ChainResidue
AARG243
AGLU312
AALA316

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1535
ChainResidue
AILE345
AASP346
AARG347
BGLN460
BSER463

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1536
ChainResidue
AGLN276
ASER348
AASP272

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1537
ChainResidue
AGLN210
AILE250
AHIS278
AGLN281
AMET282

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 1534
ChainResidue
BGLN210
BILE250
BHIS278
BGLN281
BMET282

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO C 1535
ChainResidue
CARG243
CGLU247
CALA316
DLYS323

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO D 1533
ChainResidue
CGLN460
DILE345
DASP346
DARG347
DSER348

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
AASN193
BASN193
CASN193
DASN193

site_idSWS_FT_FI2
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q13619
ChainResidueDetails
ALEU190
BLEU190
CLEU190
DLEU190

221716

PDB entries from 2024-06-26

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