eF-site ID 1znq-R
PDB Code 1znq
Chain R

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Title Crystal Structure of Human Liver GAPDH
Classification OXIDOREDUCTASE
Compound Glyceraldehyde-3-phosphate dehydrogenase, liver
Source (G3P2_HUMAN)
Sequence R:  KVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNY
MVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDP
SKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIIS
APSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAK
VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGA
LQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSV
VDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVV
SSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN
RVVDLMAHMASKE
Description


Functional site

1) chain R
residue 9
type
sequence N
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

2) chain R
residue 10
type
sequence G
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

3) chain R
residue 11
type
sequence F
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

4) chain R
residue 12
type
sequence G
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

5) chain R
residue 13
type
sequence R
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

6) chain R
residue 14
type
sequence I
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

7) chain R
residue 35
type
sequence D
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

8) chain R
residue 36
type
sequence P
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

9) chain R
residue 37
type
sequence F
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

10) chain R
residue 38
type
sequence I
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

11) chain R
residue 80
type
sequence R
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

12) chain R
residue 98
type
sequence S
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

13) chain R
residue 99
type
sequence T
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

14) chain R
residue 100
type
sequence G
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

15) chain R
residue 122
type
sequence S
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

16) chain R
residue 123
type
sequence A
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

17) chain R
residue 152
type
sequence C
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

18) chain R
residue 183
type
sequence A
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

19) chain R
residue 316
type
sequence N
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

20) chain R
residue 320
type
sequence Y
description BINDING SITE FOR RESIDUE NAD R 1003
source : AC3

21) chain R
residue 153
type ACT_SITE
sequence T
description Nucleophile => ECO:0000269|PubMed:25086035
source Swiss-Prot : SWS_FT_FI1

22) chain R
residue 76
type MOD_RES
sequence I
description Phosphothreonine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:20068231
source Swiss-Prot : SWS_FT_FI10

23) chain R
residue 84
type MOD_RES
sequence K
description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI11

24) chain R
residue 123
type MOD_RES
sequence A
description Phosphoserine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI12

25) chain R
residue 149
type MOD_RES
sequence N
description Phosphoserine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI12

26) chain R
residue 152
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI13

27) chain R
residue 153
type MOD_RES
sequence T
description S-nitrosocysteine; in reversibly inhibited form => ECO:0000250|UniProtKB:P04797
source Swiss-Prot : SWS_FT_FI14

28) chain R
residue 154
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI15

29) chain R
residue 178
type MOD_RES
sequence V
description Phosphothreonine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI16

30) chain R
residue 183
type MOD_RES
sequence A
description Phosphothreonine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI16

31) chain R
residue 185
type MOD_RES
sequence Q
description Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI17

32) chain R
residue 195
type MOD_RES
sequence L
description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771
source Swiss-Prot : SWS_FT_FI18

33) chain R
residue 216
type MOD_RES
sequence A
description N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771
source Swiss-Prot : SWS_FT_FI18

34) chain R
residue 212
type MOD_RES
sequence G
description Phosphothreonine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI19

35) chain R
residue 14
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976
source Swiss-Prot : SWS_FT_FI2

36) chain R
residue 36
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976
source Swiss-Prot : SWS_FT_FI2

37) chain R
residue 81
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976
source Swiss-Prot : SWS_FT_FI2

38) chain R
residue 123
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976
source Swiss-Prot : SWS_FT_FI2

39) chain R
residue 317
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16510976
source Swiss-Prot : SWS_FT_FI2

40) chain R
residue 228
type MOD_RES
sequence L
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI20

41) chain R
residue 230
type MOD_RES
sequence G
description Phosphothreonine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI21

42) chain R
residue 238
type MOD_RES
sequence A
description Phosphothreonine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI22

43) chain R
residue 242
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI23

44) chain R
residue 248
type MOD_RES
sequence R
description S-nitrosocysteine => ECO:0000269|PubMed:22771119, ECO:0000269|PubMed:25417112
source Swiss-Prot : SWS_FT_FI24

45) chain R
residue 313
type MOD_RES
sequence W
description Phosphoserine => ECO:0000269|PubMed:18183946, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI25

46) chain R
residue 334
type MOD_RES
sequence K
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI26

47) chain R
residue 198
type CARBOHYD
sequence D
description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:28522607
source Swiss-Prot : SWS_FT_FI27

48) chain R
residue 201
type CARBOHYD
sequence G
description (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269|PubMed:28522607
source Swiss-Prot : SWS_FT_FI27

49) chain R
residue 187
type CROSSLNK
sequence T
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI28

50) chain R
residue 183
type BINDING
sequence A
description BINDING => ECO:0000250|UniProtKB:P22513
source Swiss-Prot : SWS_FT_FI3

51) chain R
residue 212
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P22513
source Swiss-Prot : SWS_FT_FI3

52) chain R
residue 235
type BINDING
sequence V
description BINDING => ECO:0000250|UniProtKB:P22513
source Swiss-Prot : SWS_FT_FI3

53) chain R
residue 152
type BINDING
sequence C
description BINDING => ECO:0000250|UniProtKB:P22513
source Swiss-Prot : SWS_FT_FI3

54) chain R
residue 180
type SITE
sequence A
description Activates thiol group during catalysis => ECO:0000305|PubMed:16239728, ECO:0000305|PubMed:16510976
source Swiss-Prot : SWS_FT_FI4

55) chain R
residue 6
type MOD_RES
sequence V
description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI5

56) chain R
residue 67
type MOD_RES
sequence L
description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI5

57) chain R
residue 261
type MOD_RES
sequence V
description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI5

58) chain R
residue 264
type MOD_RES
sequence Q
description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI5

59) chain R
residue 335
type MOD_RES
sequence E
description N6,N6-dimethyllysine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI5

60) chain R
residue 10
type MOD_RES
sequence G
description Deamidated asparagine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI6

61) chain R
residue 65
type MOD_RES
sequence G
description Deamidated asparagine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI6

62) chain R
residue 71
type MOD_RES
sequence G
description Deamidated asparagine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI6

63) chain R
residue 150
type MOD_RES
sequence A
description Deamidated asparagine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI6

64) chain R
residue 156
type MOD_RES
sequence C
description Deamidated asparagine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI6

65) chain R
residue 226
type MOD_RES
sequence G
description Deamidated asparagine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI6

66) chain R
residue 317
type MOD_RES
sequence E
description Deamidated asparagine => ECO:0000269|PubMed:18183946
source Swiss-Prot : SWS_FT_FI6

67) chain R
residue 43
type MOD_RES
sequence M
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI7

68) chain R
residue 47
type MOD_RES
sequence F
description Methionine sulfoxide; in vitro => ECO:0000305|PubMed:25086035
source Swiss-Prot : SWS_FT_FI8

69) chain R
residue 62
type MOD_RES
sequence A
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI9

70) chain R
residue 220
type MOD_RES
sequence V
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI9

71) chain R
residue 255
type MOD_RES
sequence Y
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI9


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