eF-site ID 1ldk-ABCDE
PDB Code 1ldk
Chain A, B, C, D, E
Title Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase Complex
Classification LIGASE
Compound CULLIN HOMOLOG
Source (SKP2_HUMAN)
Sequence A:  IGLDQIWDDLRAGIQQVYTRQSMAKSRYMELYTHVYNYCT
SQFVGLELYKRLKEFLKNYLTNLLKDGEDLMDESVLKFYT
QQWEDYRFSSKVLNGICAYLNRHWVRRECKGIYEIYSLAL
VTWRDCLFRPLNKQVTNAVLKLIEKERNGETINTRLISGV
VQSYVELGLNEDLTVYKESFESQFLADTERFYTRESTEFL
QQNPVTEYMKKAEARLLEEQRRVQVYLHESTQDELARKCE
QVLIEKHLEIFHTEFQNLLDADKNEDLGRMYNLVSRIQDG
LGELKKLLETHIHNQGLAAIEKCGEAALNDPKMYVQTVLD
VHKKYNALVMSAFNNDAGFVAALDKACGRFINNNAVTK
B:  MAQSSSKSPELLARYCDSLLKKSSKNPEEAELEDTLNQVM
VVFKYIEDKDVFQKFYAKMLAKRLVHQNSASDDAEASMIS
KLKQACGFEYTSKLQRMFQDIGVSKDLNEQFKKHLTNSEP
LDLDFSIQVLSSGSWPFQQSCTFALPSELERSYQRFTAFY
ASRHSGRKLTWLYQLSKGELVTNCFKNRYTLQASTFQMAI
LLQYNTEDAYTVQQLTDSTQIKMDILAQVLQILLKSKLLV
LEDENANVDEVELKPDTLIKLYLGYKNKKLRVNINVPMKT
EQKQEQETTHKNIEEDRKLLIQAAIVRIMKMRKVLKHQQL
LGEVLTQLSSRFKPRVPVIKKCIDILIEKEYLERVDGEKD
TYSYLA
C:  KKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQA
NQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDN
REWEFQKY
D:  PSIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDPVPL
PNVNAAILKKVIQWCTHHKDDDIPVWDQEFLKVDQGTLFE
LILAANYLDIKGLLDVTCKTVANMIKGKTPEEIRKTFN
E:  WDSLPDELLLGIFSCLCLPELLKVSGVCKRWYRLASDESL
W
Description (1)  CULLIN HOMOLOG/ring-box protein 1/CYCLIN A/CDK2-ASSOCIATED PROTEIN P19/SKP2-like protein type gamma


Functional site
1) chain C
residue 1097
type
sequence D
description BINDING SITE FOR RESIDUE ZN C 4002
source : AC1
2) chain B
residue 749-776
type prosite
sequence IKKCIDILIEKEYLERVDGEKDTYSYLA
description CULLIN_1 Cullin family signature. IKkcIdiLIEKeYLeRvdgekdtYsYlA
source prosite : PS01256
3) chain C
residue 1042
type BINDING
sequence C
description 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
source Swiss-Prot : SWS_FT_FI2
4) chain C
residue 1094
type BINDING
sequence C
description 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
source Swiss-Prot : SWS_FT_FI2
5) chain C
residue 1097
type BINDING
sequence D
description 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
source Swiss-Prot : SWS_FT_FI2
6) chain C
residue 1045
type BINDING
sequence C
description 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
source Swiss-Prot : SWS_FT_FI2
7) chain C
residue 1053
type BINDING
sequence C
description 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
source Swiss-Prot : SWS_FT_FI2
8) chain C
residue 1056
type BINDING
sequence C
description 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
source Swiss-Prot : SWS_FT_FI2
9) chain C
residue 1068
type BINDING
sequence C
description 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
source Swiss-Prot : SWS_FT_FI2
10) chain C
residue 1075
type BINDING
sequence C
description 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
source Swiss-Prot : SWS_FT_FI2
11) chain C
residue 1077
type BINDING
sequence H
description 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
source Swiss-Prot : SWS_FT_FI2
12) chain C
residue 1080
type BINDING
sequence H
description 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
source Swiss-Prot : SWS_FT_FI2
13) chain C
residue 1082
type BINDING
sequence H
description 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
source Swiss-Prot : SWS_FT_FI2
14) chain C
residue 1083
type BINDING
sequence C
description 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
source Swiss-Prot : SWS_FT_FI3
15) chain D
residue 2138
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
source Swiss-Prot : SWS_FT_FI1

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