eF-site ID 3j96-ABCDEFGHIJKLM
PDB Code 3j96
Chain A, B, C, D, E, F, G, H, I, J, K, L, M
Title Structure of 20S supercomplex determined by single particle cryoelectron microscopy (State I)
Classification HYDROLASE
Compound Vesicle-fusing ATPase
Source (3J96)
Sequence A:  MAGRSMQAARCPTDELSLSNCAVVSEKDYQSGQHVIVRTS
PNHKYIFTLRTHPSVVPGSVAFSLPQRKWAGLSIGQEIEV
ALYSFDKAKQCIGTMTIEIDFLQKKNIDSNPYDTDKMAAE
FIQQFNNQAFSVGQQLVFSFNDKLFGLLVKDIEAMRQKIE
VGLVVGNSQVAFEKAENSSLNLIGKAKTFEKMGIGGLDKE
FSDIFRRAFASRVFPPEIVEQMGCKHVKGILLYGPPGCGK
TLLARQIGKMLNAREPKVVNGPEILNKYVGESEANIRKLF
ADAEEEQRRLGANSGLHIIIFDEIDAICHDTVVNQLLSKI
DGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVKMEIGLP
DEKGRLQILHIHTARMRGHQLLSADVDIKELAVETKNFSG
AELEGLVRAAQSTAMNRHIDFLASLENDIKPAFGTNQEDY
ASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRTPLVSV
LLEGPPHSGKTALAAKIAEESNFPFIKICSPDKMIGFSET
AKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYVPIGPRFS
NLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQEMEMLN
AFSTTIHVPNIATGEQLLEALELLGNFKDKERTTIAQQVK
GKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLALLREEG
B:  MAGRSMQAARCPTDELSLSNCAVVSEKDYQSGQHVIVRTS
PNHKYIFTLRTHPSVVPGSVAFSLPQRKWAGLSIGQEIEV
ALYSFDKAKQCIGTMTIEIDFLQKKNIDSNPYDTDKMAAE
FIQQFNNQAFSVGQQLVFSFNDKLFGLLVKDIEAMRQKIE
VGLVVGNSQVAFEKAENSSLNLIGKAKTKMGIGGLDKEFS
DIFRRAFASRVFPPEIVEQMGCKHVKGILLYGPPGCGKTL
LARQIGKMLNAREPKVVNGPEILNKYVGESEANIRKLFAD
AEEEQRRLGANSGLHIIIFDEIHDTVVNQLLSKIDGVEQL
NNILVIGMTNRPDLIDEALLRPGRLEVKMEIGLPDEKGRL
QILHIHTARMRGHQLLSADVDIKELAVETKNFSGAELEGL
VRAAQSTAMNRHIDFLASLENDIKPAFGTNQEDYASYIMN
GIIKWGDPVTRVLDDGELLVQQTKNSDRTPLVSVLLEGPP
HSGKTALAAKIAEESNFPFIKICSPDKMIGFSETAKCQAM
KKIFDDAYKSQLSCVVVDDIERLLDYVPIGPRFSNLVLQA
LLVLLKKAPPQGRKLLIIGTTSRKDVLQEMEMLNAFSTTI
HVPNIATGEQLLEALELLGNFKDKERTTIAQQVKGKKVWI
GIKKLLMLIEMSLQMDPEYRVRKFLALLREEG
C:  MAGRSMQAARCPTDELSLSNCAVVSEKDYQSGQHVIVRTS
PNHKYIFTLRTHPSVVPGSVAFSLPQRKWAGLSIGQEIEV
ALYSFDKAKQCIGTMTIEIDFLQKKNIDSNPYDTDKMAAE
FIQQFNNQAFSVGQQLVFSFNDKLFGLLVKDIEAMRQKIE
VGLVVGNSQVAFEKAENSSLNLIGKAKTKMGIGGLDKEFS
DIFRRAFASRVFPPEIVEQMGCKHVKGILLYGPPGCGKTL
LARQIGKMLNAREPKVVNGPEILNKYVGESEANIRKLFAD
AEEEQRRLGANSGLHIIIFDEIDAICHDTVVNQLLSKIDG
VEQLNNILVIGMTNRPDLIDEALLRPGRLEVKMEIGLPDE
KGRLQILHIHTARMRGHQLLSADVDIKELAVETKNFSGAE
LEGLVRAAQSTAMNRHIDFLASLENDIKPAFGTNQEDYAS
YIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRTPLVSVLL
EGPPHSGKTALAAKIAEESNFPFIKICSPDKMIGFSETAK
CQAMKKIFDDAYKSQLSCVVVDDIERLLDYVPIGPRFSNL
VLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQEMEMLNAF
STTIHVPNIATGEQLLEALELLGNFKDKERTTIAQQVKGK
KVWIGIKKLLMLIEMSLQMDPEYRVRKFLALLREEG
D:  MAGRSMQAARCPTDELSLSNCAVVSEKDYQSGQHVIVRTS
PNHKYIFTLRTHPSVVPGSVAFSLPQRKWAGLSIGQEIEV
ALYSFDKAKQCIGTMTIEIDFLQKKNIDSNPYDTDKMAAE
FIQQFNNQAFSVGQQLVFSFNDKLFGLLVKDIEAMRQKIE
VGLVVGNSQVAFEKAENSSLNLIGKAKTKMGIGGLDKEFS
DIFRRAFASRVFPPEIVEQMGCKHVKGILLYGPPGCGKTL
LARQIGKMLNAREPKVVNGPEILNKYVGESEANIRKLFAD
AEEEQRRLGANSGLHIIIFDEIDAIDTVVNQLLSKIDGVE
QLNNILVIGMTNRPDLIDEALLRPGRLEVKMEIGLPDEKG
RLQILHIHTARMRGHQLLSADVDIKELAVETKNFSGAELE
GLVRAAQSTAMNRHIFLASLENDIKPAFGTNQEDYASYIM
NGIIKWGDPVTRVLDDGELLVQQTKNSDRTPLVSVLLEGP
PHSGKTALAAKIAEESNFPFIKICSPDKMIGFSETAKCQA
MKKIFDDAYKSQLSCVVVDDIERLLDYVPIGPRFSNLVLQ
ALLVLLKKAPPQGRKLLIIGTTSRKDVLQEMEMLNAFSTT
IHVPNIATGEQLLEALELLGNFKDKERTTIAQQVKGKKVW
IGIKKLLMLIEMSLQMDPEYRVRKFLALLREEG
E:  MAGRSMQAARCPTDELSLSNCAVVSEKDYQSGQHVIVRTS
PNHKYIFTLRTHPSVVPGSVAFSLPQRKWAGLSIGQEIEV
ALYSFDKAKQCIGTMTIEIDFLQKKNIDSNPYDTDKMAAE
FIQQFNNQAFSVGQQLVFSFNDKLFGLLVKDIEAMRQKIE
VGLVVGNSQVAFEKAENSSLNLIGKAKTKMGIGGLDKEFS
DIFRRAFASRVFPPEIVEQMGCKHVKGILLYGPPGCGKTL
LARQIGKMLNAREPKVVNGPEILNKYVGESEANIRKLFAD
AEEEQRRLGANSGLHIIIFDEIHDTVVNQLLSKIDGVEQL
NNILVIGMTNRPDLIDEALLRPGRLEVKMEIGLPDEKGRL
QILHIHTARMRGHQLLSADVDIKELAVETKNFSGAELEGL
VRAAQSTAMNRHIDFLASLENDIKPAFGTEDYASYIMNGI
IKWGDPVTRVLDDGELLVQQTKNSDRTPLVSVLLEGPPHS
GKTALAAKIAEESNFPFIKICSPDKMIGFSETAKCQAMKK
IFDDAYKSQLSCVVVDDIERLLDYVPIGPRFSNLVLQALL
VLLKKAPPQGRKLLIIGTTSRKDVLQEMEMLNAFSTTIHV
PNIATGEQLLEALELLGNFKDKERTTIAQQVKGKKVWIGI
KKLLMLIEMSLQMDPEYRVRKFLALLREEG
F:  MAGRSMQAARCPTDELSLSNCAVVSEKDYQSGQHVIVRTS
PNHKYIFTLRTHPSVVPGSVAFSLPQRKWAGLSIGQEIEV
ALYSFDKAKQCIGTMTIEIDFLQKKNIDSNPYDTDKMAAE
FIQQFNNQAFSVGQQLVFSFNDKLFGLLVKDIEAMRQKIE
VGLVVGNSQVAFEKAENSSLNLIGKAKTKMGIGGLDKEFS
DIFRRAFASRVFPPEIVEQMGCKHVKGILLYGPPGCGKTL
LARQIGKMLNAREPKVVNGPEILNKYVGESEANIRKLFAD
AEEEQRRLGANSGLHIIIFDEIHDTVVNQLLSKIDGVEQL
NNILVIGMTNRPDLIDEALLRPGRLEVKMEIGLPDEKGRL
QILHIHTARMRGHQLLSADVDIKELAVETKNFSGAELEGL
VRAAQSTAMNRHIEDYASYIMNGIIKWGDPVTRVLDDGEL
LVQQTKNSDRTPLVSVLLEGPPHSGKTALAAKIAEESNFP
FIKICSPDKMIGFSETAKCQAMKKIFDDAYKSQLSCVVVD
DIERLLDYVPIGPRFSNLVLQALLVLLKKAPPQGRKLLII
GTTSRKDVLQEMEMLNAFSTTIHVPNIATGEQLLEALELL
GNFKDKERTTIAQQVKGKKVWIGIKKLLMLIEMSLQMDPE
YRVRKFLALLREEG
G:  AEAMALLAEAERKVKNSQSFFSGLFGGSSKIEEACEIYAR
AANMFKMAKNWSAAGNAFCQAAQLHLQLQSKHDAATCFVD
AGNAFKKADPQEAINCLMRAIEIYTDMGRFTIAAKHHISI
AEIYETELVDVEKAIAHYEQSADYYKGEESNSSANKCLLK
VAGYAAQLEQYQKAIDIYEQVGTSAMDSPLLKYSAKDYFF
KAALCHFCIDMLNAKLAVQKYEELFPAFSDSRECKLMKKL
LEAHEEQNVDSYTESVKEYDSISRLDQWLTTMLLRIKKTI
QGDEED
H:  AEAMALLAEAERKVKNSQSFFSGLFGGSSKIEEACEIYAR
AANMFKMAKNWSAAGNAFCQAAQLHLQLQSKHDAATCFVD
AGNAFKKADPQEAINCLMRAIEIYTDMGRFTIAAKHHISI
AEIYETELVDVEKAIAHYEQSADYYKGEESNSSANKCLLK
VAGYAAQLEQYQKAIDIYEQVGTSAMDSPLLKYSAKDYFF
KAALCHFCIDMLNAKLAVQKYEELFPAFSDSRECKLMKKL
LEAHEEQNVDSYTESVKEYDSISRLDQWLTTMLLRIKKTI
QGDEED
I:  AEAMALLAEAERKVKNSQSFFSGLFGGSSKIEEACEIYAR
AANMFKMAKNWSAAGNAFCQAAQLHLQLQSKHDAATCFVD
AGNAFKKADPQEAINCLMRAIEIYTDMGRFTIAAKHHISI
AEIYETELVDVEKAIAHYEQSADYYKGEESNSSANKCLLK
VAGYAAQLEQYQKAIDIYEQVGTSAMDSPLLKYSAKDYFF
KAALCHFCIDMLNAKLAVQKYEELFPAFSDSRECKLMKKL
LEAHEEQNVDSYTESVKEYDSISRLDQWLTTMLLRIKKTI
QGDEED
J:  AEAMALLAEAERKVKNSQSFFSGLFGGSSKIEEACEIYAR
AANMFKMAKNWSAAGNAFCQAAQLHLQLQSKHDAATCFVD
AGNAFKKADPQEAINCLMRAIEIYTDMGRFTIAAKHHISI
AEIYETELVDVEKAIAHYEQSADYYKGEESNSSANKCLLK
VAGYAAQLEQYQKAIDIYEQVGTSAMDSPLLKYSAKDYFF
KAALCHFCIDMLNAKLAVQKYEELFPAFSDSRECKLMKKL
LEAHEEQNVDSYTESVKEYDSISRLDQWLTTMLLRIKKTI
QGDEED
K:  NRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRAD
ALQAGASQFETSAAKLKRKYW
L:  ALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMI
DRIEYNVEHAVDYVERAVSDTKKAVK
M:  RADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQ
LDRVEEGMNHINQDMKEAEKNLKDLGKARENEMDENLEQV
SGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRID
EANQRATKMLG
Description


Functional site
1) chain A
residue 549
type catalytic
sequence K
description 642
source MCSA : MCSA1
2) chain A
residue 550
type catalytic
sequence T
description 642
source MCSA : MCSA1
3) chain A
residue 603
type catalytic
sequence D
description 642
source MCSA : MCSA1
4) chain A
residue 604
type catalytic
sequence D
description 642
source MCSA : MCSA1
5) chain A
residue 631
type catalytic
sequence K
description 642
source MCSA : MCSA1
6) chain A
residue 708
type catalytic
sequence K
description 642
source MCSA : MCSA1
7) chain B
residue 549
type catalytic
sequence K
description 642
source MCSA : MCSA2
8) chain B
residue 550
type catalytic
sequence T
description 642
source MCSA : MCSA2
9) chain B
residue 603
type catalytic
sequence D
description 642
source MCSA : MCSA2
10) chain B
residue 604
type catalytic
sequence D
description 642
source MCSA : MCSA2
11) chain B
residue 631
type catalytic
sequence K
description 642
source MCSA : MCSA2
12) chain B
residue 708
type catalytic
sequence K
description 642
source MCSA : MCSA2
13) chain C
residue 549
type catalytic
sequence K
description 642
source MCSA : MCSA3
14) chain C
residue 550
type catalytic
sequence T
description 642
source MCSA : MCSA3
15) chain C
residue 603
type catalytic
sequence D
description 642
source MCSA : MCSA3
16) chain C
residue 604
type catalytic
sequence D
description 642
source MCSA : MCSA3
17) chain C
residue 631
type catalytic
sequence K
description 642
source MCSA : MCSA3
18) chain C
residue 708
type catalytic
sequence K
description 642
source MCSA : MCSA3
19) chain D
residue 549
type catalytic
sequence K
description 642
source MCSA : MCSA4
20) chain D
residue 550
type catalytic
sequence T
description 642
source MCSA : MCSA4
21) chain D
residue 603
type catalytic
sequence D
description 642
source MCSA : MCSA4
22) chain D
residue 604
type catalytic
sequence D
description 642
source MCSA : MCSA4
23) chain D
residue 631
type catalytic
sequence K
description 642
source MCSA : MCSA4
24) chain D
residue 708
type catalytic
sequence K
description 642
source MCSA : MCSA4
25) chain E
residue 549
type catalytic
sequence K
description 642
source MCSA : MCSA5
26) chain E
residue 550
type catalytic
sequence T
description 642
source MCSA : MCSA5
27) chain E
residue 603
type catalytic
sequence D
description 642
source MCSA : MCSA5
28) chain E
residue 604
type catalytic
sequence D
description 642
source MCSA : MCSA5
29) chain E
residue 631
type catalytic
sequence K
description 642
source MCSA : MCSA5
30) chain E
residue 708
type catalytic
sequence K
description 642
source MCSA : MCSA5
31) chain F
residue 549
type catalytic
sequence K
description 642
source MCSA : MCSA6
32) chain F
residue 550
type catalytic
sequence T
description 642
source MCSA : MCSA6
33) chain F
residue 603
type catalytic
sequence D
description 642
source MCSA : MCSA6
34) chain F
residue 604
type catalytic
sequence D
description 642
source MCSA : MCSA6
35) chain F
residue 631
type catalytic
sequence K
description 642
source MCSA : MCSA6
36) chain F
residue 708
type catalytic
sequence K
description 642
source MCSA : MCSA6
37) chain K
residue 49-68
type prosite
sequence NVDKVLERDQKLSELDDRAD
description SYNAPTOBREVIN Synaptobrevin signature. NVDKVlERdqKLSeLdDRAD
source prosite : PS00417
38) chain A
residue 367-385
type prosite
sequence ILVIGMTNRPDLIDEALLR
description AAA AAA-protein family signature. IlVIgMTNrpdlIDeALl.R
source prosite : PS00674
39) chain L
residue 198-237
type prosite
sequence RHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNV
description SYNTAXIN Syntaxin / epimorphin family signature. RhseIikLEnsIrELhdMFmdMamlVesQGemIDrIEyn.V
source prosite : PS00914
40) chain M
residue 180
type SITE
sequence R
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI1
41) chain E
residue 545
type SITE
sequence P
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI1
42) chain F
residue 505
type SITE
sequence N
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI1
43) chain F
residue 545
type SITE
sequence P
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI1
44) chain C
residue 505
type SITE
sequence N
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI1
45) chain C
residue 545
type SITE
sequence P
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI1
46) chain D
residue 505
type SITE
sequence N
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI1
47) chain D
residue 545
type SITE
sequence P
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI1
48) chain E
residue 505
type SITE
sequence N
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI1
49) chain M
residue 197
type SITE
sequence Q
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI2
50) chain H
residue 26
type SITE
sequence S
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI2
51) chain L
residue 253
type SITE
sequence K
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI2
52) chain L
residue 256
type SITE
sequence K
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI2
53) chain E
residue 550
type SITE
sequence T
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI2
54) chain F
residue 550
type SITE
sequence T
description (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915
source Swiss-Prot : SWS_FT_FI2
55) chain G
residue 195
type MOD_RES
sequence S
description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461
source Swiss-Prot : SWS_FT_FI3
56) chain H
residue 29
type MOD_RES
sequence S
description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461
source Swiss-Prot : SWS_FT_FI3
57) chain H
residue 195
type MOD_RES
sequence S
description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461
source Swiss-Prot : SWS_FT_FI3
58) chain I
residue 29
type MOD_RES
sequence S
description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461
source Swiss-Prot : SWS_FT_FI3
59) chain I
residue 195
type MOD_RES
sequence S
description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461
source Swiss-Prot : SWS_FT_FI3
60) chain J
residue 29
type MOD_RES
sequence S
description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461
source Swiss-Prot : SWS_FT_FI3
61) chain J
residue 195
type MOD_RES
sequence S
description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461
source Swiss-Prot : SWS_FT_FI3
62) chain M
residue 154
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P60879
source Swiss-Prot : SWS_FT_FI4
63) chain M
residue 187
type MOD_RES
sequence S
description Phosphoserine; by PKC => ECO:0000269|PubMed:12459461
source Swiss-Prot : SWS_FT_FI5
64) chain B
residue 259
type MOD_RES
sequence Y
description Phosphoserine; by PKC => ECO:0000269|PubMed:12459461
source Swiss-Prot : SWS_FT_FI5
65) chain C
residue 259
type MOD_RES
sequence Y
description Phosphoserine; by PKC => ECO:0000269|PubMed:12459461
source Swiss-Prot : SWS_FT_FI5
66) chain D
residue 259
type MOD_RES
sequence Y
description Phosphoserine; by PKC => ECO:0000269|PubMed:12459461
source Swiss-Prot : SWS_FT_FI5
67) chain E
residue 259
type MOD_RES
sequence Y
description Phosphoserine; by PKC => ECO:0000269|PubMed:12459461
source Swiss-Prot : SWS_FT_FI5
68) chain F
residue 259
type MOD_RES
sequence Y
description Phosphoserine; by PKC => ECO:0000269|PubMed:12459461
source Swiss-Prot : SWS_FT_FI5
69) chain E
residue 569
type LIPID
sequence S
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P60879
source Swiss-Prot : SWS_FT_FI6
70) chain F
residue 569
type LIPID
sequence S
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P60879
source Swiss-Prot : SWS_FT_FI6

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