eF-site ID 1bg3-AB
PDB Code 1bg3
Chain A, B

click to enlarge
Title RAT BRAIN HEXOKINASE TYPE I COMPLEX WITH GLUCOSE AND INHIBITOR GLUCOSE-6-PHOSPHATE
Classification HEXOKINASE
Compound HEXOKINASE
Source ORGANISM_COMMON: Norway rat; ORGANISM_SCIENTIFIC: Rattus norvegicus;
Sequence A:  MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDEILIDIL
TRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDF
IALDLGGSSFRILRVQVNVSMESEIYDTPENIVHGSGTQL
FDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEA
VLITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAV
VNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHID
LVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDRELDRGSL
NPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITP
ELLTRGKFNTSDVSAIEKDKEGIQNAKEILTRLGVEPSDV
DCVSVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRL
RTTVGVDGSLYKMHPQYSRRFHKTLRRLVPDSDVRFLLSE
SGTGKGAAMVTAVAYRLAEQHRQIEETLAHFRLSKQTLME
VKKRLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHG
DFLALDLGGTNFRVLLVKIRSRTVEMHNKIYSIPLEIMQG
TGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQT
NLDCGILISWTKGFKATDCEGHDVASLLRDAVKRREEFDL
DVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEE
MKNVEMVEGNQGQMCINMEWGAFGDNGCLDDIRTDFDKVV
DEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFR
GQISEPLKTRGIFETKFLSQIESDRLALLQVRAILQQLGL
NSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENR
GLDHLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCTVS
FLLSEDGSGKGAALITAVGVRL
B:  MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDEILIDIL
TRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDF
IALDLGGSSFRILRVQVNVSMESEIYDTPENIVHGSGTQL
FDHVADCLGDFMEKKDKKLPVGFTFSFPCRQSKIDEAVLI
TWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVND
TVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVE
GDEGRMCINTEWGAFGDDGSLEDIRTEFDRELDRGSLNPG
KQLFEKMVSGMYMGELVRLILVKMAKEGLLFEGRITPELL
TRGKFNTSDVSAIEKDKEGIQNAKEILTRLGVEPSDVDCV
SVQHICTIVSFRSANLVAATLGAILNRLRDNKGTPRLRTT
VGVDGSLYKMHPQYSRRFHKTLRRLVPDSDVRFLLSESGT
GKGAAMVTAVAYRLAEQHRQIEETLAHFRLSKQTLMEVKK
RLRTEMEMGLRKETNSKATVKMLPSFVRSIPDGTEHGDFL
ALDLGGTNFRVLLVKIRSGKKRTVEMHNKIYSIPLEIMQG
TGDELFDHIVSCISDFLDYMGIKGPRMPLGFTFSFPCHQT
NLDCGILISWTKGFKATDCEGHDVASLLRDAVKRREEFDL
DVVAVVNDTVGTMMTCAYEEPTCEIGLIVGTGTNACYMEE
MKNVEMVEGNQGQMCINMEWGAFGDNGCLDDIRTDFDKVV
DEYSLNSGKQRFEKMISGMYLGEIVRNILIDFTKKGFLFR
GQISEPLKTRGIFETKFLSQIESDRLALLQVRAILQQLGL
NSTCDDSILVKTVCGVVSKRAAQLCGAGMAAVVEKIRENR
GLDHLNVTVGVDGTLYKLHPHFSRIMHQTVKELSPKCTVS
FLLSEDGSGKGAALITAVGVRL
Description


Functional site

1) chain A
residue 150-175
type prosite
sequence VGFTFSFPCRQSKIDEAVLITWTKRF
description HEXOKINASE_1 Hexokinase domain signature. VGFTFSFPcrqskIDeavLitWTKrF
source prosite : PS00378

2) chain A
residue 598-623
type prosite
sequence LGFTFSFPCHQTNLDCGILISWTKGF
description HEXOKINASE_1 Hexokinase domain signature. VGFTFSFPcrqskIDeavLitWTKrF
source prosite : PS00378

3) chain A
residue 30
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P19367
source Swiss-Prot : SWS_FT_FI1

4) chain B
residue 863
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P19367
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 425
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P19367
source Swiss-Prot : SWS_FT_FI1

6) chain A
residue 747
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P19367
source Swiss-Prot : SWS_FT_FI1

7) chain A
residue 784
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P19367
source Swiss-Prot : SWS_FT_FI1

8) chain A
residue 863
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P19367
source Swiss-Prot : SWS_FT_FI1

9) chain B
residue 30
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P19367
source Swiss-Prot : SWS_FT_FI1

10) chain B
residue 425
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P19367
source Swiss-Prot : SWS_FT_FI1

11) chain B
residue 747
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P19367
source Swiss-Prot : SWS_FT_FI1

12) chain B
residue 784
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P19367
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 84
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

14) chain A
residue 413
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

15) chain A
residue 449
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

16) chain A
residue 532
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

17) chain A
residue 603
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

18) chain A
residue 620
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

19) chain A
residue 656
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

20) chain A
residue 657
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

21) chain A
residue 680
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

22) chain A
residue 683
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

23) chain A
residue 708
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

24) chain A
residue 155
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

25) chain A
residue 742
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 861
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

27) chain A
residue 897
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

28) chain B
residue 84
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

29) chain B
residue 155
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

30) chain B
residue 172
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 208
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 209
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

33) chain B
residue 232
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

34) chain B
residue 235
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

35) chain A
residue 172
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

36) chain B
residue 260
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

37) chain B
residue 291
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

38) chain B
residue 413
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

39) chain B
residue 449
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

40) chain B
residue 532
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

41) chain B
residue 603
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

42) chain B
residue 620
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

43) chain B
residue 656
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

44) chain B
residue 657
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

45) chain B
residue 680
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 208
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

47) chain B
residue 683
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

48) chain B
residue 708
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

49) chain B
residue 742
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

50) chain B
residue 861
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

51) chain B
residue 897
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

52) chain A
residue 209
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

53) chain A
residue 232
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

54) chain A
residue 235
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

55) chain A
residue 260
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

56) chain A
residue 291
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:9665168, ECO:0007744|PDB:1BG3
source Swiss-Prot : SWS_FT_FI2

57) chain A
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000250|UniProtKB:P19367
source Swiss-Prot : SWS_FT_FI3

58) chain B
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000250|UniProtKB:P19367
source Swiss-Prot : SWS_FT_FI3

59) chain A
residue 337
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI4

60) chain B
residue 337
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI4


Display surface

Download
Links