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1LDK

Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0006511biological_processubiquitin-dependent protein catabolic process
A0031625molecular_functionubiquitin protein ligase binding
B0006511biological_processubiquitin-dependent protein catabolic process
B0031461cellular_componentcullin-RING ubiquitin ligase complex
B0031625molecular_functionubiquitin protein ligase binding
C0008270molecular_functionzinc ion binding
D0006511biological_processubiquitin-dependent protein catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ZN C 4002
ChainResidue
CASP1097

Functional Information from PROSITE/UniProt
site_idPS01256
Number of Residues28
DetailsCULLIN_1 Cullin family signature. IKkcIdiLIEKeYLeRvdgekdtYsYlA
ChainResidueDetails
BILE749-ALA776

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
DTHR2138

site_idSWS_FT_FI2
Number of Residues11
DetailsBINDING: BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DPL, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
ChainResidueDetails
CCYS1042
CCYS1045
CCYS1053
CCYS1056
CCYS1068
CCYS1075
CHIS1077
CHIS1080
CHIS1082
CCYS1094
CASP1097

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:11961546, ECO:0007744|PDB:1LDJ, ECO:0007744|PDB:1LDK, ECO:0007744|PDB:1U6G, ECO:0007744|PDB:2HYE, ECO:0007744|PDB:3DQV, ECO:0007744|PDB:3RTR, ECO:0007744|PDB:4F52, ECO:0007744|PDB:4P5O
ChainResidueDetails
CCYS1083

218500

PDB entries from 2024-04-17

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