eF-site ID 6bw6-C
PDB Code 6bw6
Chain C

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Title Human GPT (DPAGT1) H129 variant in complex with tunicamycin
Classification TRANSFERASE/ANTIBIOTIC
Compound UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
Source (GPT_HUMAN)
Sequence C:  PMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLN
KTSRQQIPESQGVISGAVFLIILFCFIPFPFLNCAFPHHE
FVALIGALLAICCMIFLGFADDVLNLRWRHKLLLHTAASL
PLLMVYFTNFGNTTIVHLDLGILYYVYMGLLAVFCTNAIN
ILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFSL
YFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVV
GILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIP
RLNIKTGKLEMSYSKFKTKSLSFLGTFILKVAESLQLVTV
HQCNNMTLINLLLKVLGPIHERNLTLLLLLLQILGSAITF
SIRYQ
Description


Functional site

1) chain C
residue 44
type
sequence Q
description binding site for residue TUM C 501
source : AC5

2) chain C
residue 45
type
sequence D
description binding site for residue TUM C 501
source : AC5

3) chain C
residue 46
type
sequence L
description binding site for residue TUM C 501
source : AC5

4) chain C
residue 122
type
sequence W
description binding site for residue TUM C 501
source : AC5

5) chain C
residue 185
type
sequence N
description binding site for residue TUM C 501
source : AC5

6) chain C
residue 186
type
sequence I
description binding site for residue TUM C 501
source : AC5

7) chain C
residue 188
type
sequence A
description binding site for residue TUM C 501
source : AC5

8) chain C
residue 189
type
sequence G
description binding site for residue TUM C 501
source : AC5

9) chain C
residue 190
type
sequence I
description binding site for residue TUM C 501
source : AC5

10) chain C
residue 191
type
sequence N
description binding site for residue TUM C 501
source : AC5

11) chain C
residue 249
type
sequence F
description binding site for residue TUM C 501
source : AC5

12) chain C
residue 252
type
sequence D
description binding site for residue TUM C 501
source : AC5

13) chain C
residue 293
type
sequence L
description binding site for residue TUM C 501
source : AC5

14) chain C
residue 301
type
sequence R
description binding site for residue TUM C 501
source : AC5

15) chain C
residue 302
type
sequence H
description binding site for residue TUM C 501
source : AC5

16) chain C
residue 303
type
sequence R
description binding site for residue TUM C 501
source : AC5

17) chain C
residue 304
type
sequence I
description binding site for residue TUM C 501
source : AC5

18) chain C
residue 107
type
sequence C
description binding site for residue PGW C 502
source : AC6

19) chain C
residue 110
type
sequence F
description binding site for residue PGW C 502
source : AC6

20) chain C
residue 114
type
sequence A
description binding site for residue PGW C 502
source : AC6

21) chain C
residue 118
type
sequence L
description binding site for residue PGW C 502
source : AC6

22) chain C
residue 124
type
sequence H
description binding site for residue PGW C 502
source : AC6

23) chain C
residue 28
type
sequence L
description binding site for residue PGW C 503
source : AC7

24) chain C
residue 31
type
sequence A
description binding site for residue PGW C 503
source : AC7

25) chain C
residue 32
type
sequence F
description binding site for residue PGW C 503
source : AC7

26) chain C
residue 35
type
sequence H
description binding site for residue PGW C 503
source : AC7

27) chain C
residue 68
type
sequence I
description binding site for residue PGW C 503
source : AC7

28) chain C
residue 71
type
sequence F
description binding site for residue PGW C 503
source : AC7

29) chain C
residue 56
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:30388443
source Swiss-Prot : SWS_FT_FI13

30) chain C
residue 191
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:30388443
source Swiss-Prot : SWS_FT_FI13

31) chain C
residue 301
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:30388443
source Swiss-Prot : SWS_FT_FI13

32) chain C
residue 44
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:30388443
source Swiss-Prot : SWS_FT_FI13

33) chain C
residue 46
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6
source Swiss-Prot : SWS_FT_FI14

34) chain C
residue 303
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6
source Swiss-Prot : SWS_FT_FI14

35) chain C
residue 79-91
type TOPO_DOM
sequence LNCAFP
description Lumenal => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI1

36) chain C
residue 144-166
type TOPO_DOM
sequence FGNTTIVHLDLG
description Lumenal => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI1

37) chain C
residue 214-218
type TOPO_DOM
sequence EGDCR
description Lumenal => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI1

38) chain C
residue 270-271
type TOPO_DOM
sequence HF
description Lumenal => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI1

39) chain C
residue 251-269
type TRANSMEM
sequence GDTFCYFAGMTFAVVGILG
description Helical; Name=Helix 8 => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI10

40) chain C
residue 272-293
type TRANSMEM
sequence SKTMLLFFMPQVFNFLYSLPQL
description Helical; Name=Helix 9 => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI11

41) chain C
residue 376-400
type TRANSMEM
sequence ERNLTLLLLLLQILGSAITFSIRYQ
description Helical; Name=Helix 10 => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI12

42) chain C
residue 119
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5
source Swiss-Prot : SWS_FT_FI15

43) chain C
residue 252
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5
source Swiss-Prot : SWS_FT_FI15

44) chain C
residue 125
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:30388443
source Swiss-Prot : SWS_FT_FI16

45) chain C
residue 178
type BINDING
sequence V
description BINDING => ECO:0000305|PubMed:30388443
source Swiss-Prot : SWS_FT_FI16

46) chain C
residue 59-78
type TRANSMEM
sequence GVISGAVFLIILFCFIPFPF
description Helical; Name=Helix 2 => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI4

47) chain C
residue 146
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI18

48) chain C
residue 11-38
type TRANSMEM
sequence LLINLIVSLLGFVATVTLIPAFRGHFIA
description Helical; Name=Helix 1 => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI2

49) chain C
residue 39-58
type TOPO_DOM
sequence ARLCGQDLNKTSRQQIPESQ
description Cytoplasmic => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI3

50) chain C
residue 119-121
type TOPO_DOM
sequence NLR
description Cytoplasmic => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI3

51) chain C
residue 187-192
type TOPO_DOM
sequence LAGING
description Cytoplasmic => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI3

52) chain C
residue 243-250
type TOPO_DOM
sequence WYPSRVFV
description Cytoplasmic => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI3

53) chain C
residue 294-375
type TOPO_DOM
sequence LHIIPCPRHRIPRLNIKTGKLEMSYSKFKTKSLSFLGTFI
LKVAESLQLVTVHQCNNMTLINLLLKVLGPIH
description Cytoplasmic => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI3

54) chain C
residue 92-118
type TRANSMEM
sequence HHEFVALIGALLAICCMIFLGFADDVL
description Helical; Name=Helix 3 => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI5

55) chain C
residue 122-143
type TRANSMEM
sequence WRHKLLLHTAASLPLLMVYFTN
description Helical; Name=Helix 4 => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI6

56) chain C
residue 167-186
type TRANSMEM
sequence ILYYVYMGLLAVFCTNAINI
description Helical; Name=Helix 5 => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI7

57) chain C
residue 193-213
type TRANSMEM
sequence LEAGQSLVISASIIVFNLVEL
description Helical; Name=Helix 6 => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI8

58) chain C
residue 219-242
type TRANSMEM
sequence DDHVFSLYFMIPFFFTTLGLLYHN
description Helical; Name=Helix 7 => ECO:0000269|PubMed:29459785
source Swiss-Prot : SWS_FT_FI9

59) chain C
residue 185
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW6
source Swiss-Prot : SWS_FT_FI17


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