eF-site ID 4coo-AB
PDB Code 4coo
Chain A, B

click to enlarge
Title Crystal structure of human cystathionine beta-synthase (delta516-525) at 2.0 angstrom resolution
Classification LYASE
Compound CYSTATHIONINE BETA-SYNTHASE
Source Homo sapiens (Human) (CBS_HUMAN)
Sequence A:  WIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILK
KIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRI
SLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRG
YRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPES
HVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQ
QCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDP
EGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDK
WFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQ
ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDL
TEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKG
FDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKV
IYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQMVFGVVT
AIDLLNFVAAQER
B:  WIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILK
KIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRI
SLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRG
YRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPES
HVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQ
QCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDP
EGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDK
WFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQ
ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKKPWW
WHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVV
DEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQ
IRLTDTLGRLSHILEMDHFALVVHEQQMVFGVVTAIDLLN
FVAAQER
Description


Functional site

1) chain A
residue 50
type
sequence S
description BINDING SITE FOR RESIDUE HEM A 1549
source : AC1

2) chain A
residue 51
type
sequence R
description BINDING SITE FOR RESIDUE HEM A 1549
source : AC1

3) chain A
residue 52
type
sequence C
description BINDING SITE FOR RESIDUE HEM A 1549
source : AC1

4) chain A
residue 53
type
sequence T
description BINDING SITE FOR RESIDUE HEM A 1549
source : AC1

5) chain A
residue 54
type
sequence W
description BINDING SITE FOR RESIDUE HEM A 1549
source : AC1

6) chain A
residue 62
type
sequence E
description BINDING SITE FOR RESIDUE HEM A 1549
source : AC1

7) chain A
residue 63
type
sequence S
description BINDING SITE FOR RESIDUE HEM A 1549
source : AC1

8) chain A
residue 64
type
sequence P
description BINDING SITE FOR RESIDUE HEM A 1549
source : AC1

9) chain A
residue 65
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 1549
source : AC1

10) chain A
residue 224
type
sequence R
description BINDING SITE FOR RESIDUE HEM A 1549
source : AC1

11) chain A
residue 226
type
sequence A
description BINDING SITE FOR RESIDUE HEM A 1549
source : AC1

12) chain A
residue 230
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 1549
source : AC1

13) chain A
residue 233
type
sequence Y
description BINDING SITE FOR RESIDUE HEM A 1549
source : AC1

14) chain A
residue 266
type
sequence R
description BINDING SITE FOR RESIDUE HEM A 1549
source : AC1

15) chain B
residue 50
type
sequence S
description BINDING SITE FOR RESIDUE HEM B 1539
source : AC2

16) chain B
residue 51
type
sequence R
description BINDING SITE FOR RESIDUE HEM B 1539
source : AC2

17) chain B
residue 52
type
sequence C
description BINDING SITE FOR RESIDUE HEM B 1539
source : AC2

18) chain B
residue 53
type
sequence T
description BINDING SITE FOR RESIDUE HEM B 1539
source : AC2

19) chain B
residue 59
type
sequence P
description BINDING SITE FOR RESIDUE HEM B 1539
source : AC2

20) chain B
residue 62
type
sequence E
description BINDING SITE FOR RESIDUE HEM B 1539
source : AC2

21) chain B
residue 63
type
sequence S
description BINDING SITE FOR RESIDUE HEM B 1539
source : AC2

22) chain B
residue 64
type
sequence P
description BINDING SITE FOR RESIDUE HEM B 1539
source : AC2

23) chain B
residue 65
type
sequence H
description BINDING SITE FOR RESIDUE HEM B 1539
source : AC2

24) chain B
residue 226
type
sequence A
description BINDING SITE FOR RESIDUE HEM B 1539
source : AC2

25) chain B
residue 229
type
sequence P
description BINDING SITE FOR RESIDUE HEM B 1539
source : AC2

26) chain B
residue 233
type
sequence Y
description BINDING SITE FOR RESIDUE HEM B 1539
source : AC2

27) chain B
residue 266
type
sequence R
description BINDING SITE FOR RESIDUE HEM B 1539
source : AC2

28) chain A
residue 119
type
sequence K
description BINDING SITE FOR RESIDUE ACT A 1550
source : AC3

29) chain A
residue 146
type
sequence T
description BINDING SITE FOR RESIDUE ACT A 1550
source : AC3

30) chain A
residue 147
type
sequence S
description BINDING SITE FOR RESIDUE ACT A 1550
source : AC3

31) chain A
residue 149
type
sequence N
description BINDING SITE FOR RESIDUE ACT A 1550
source : AC3

32) chain A
residue 150
type
sequence T
description BINDING SITE FOR RESIDUE ACT A 1550
source : AC3

33) chain A
residue 222
type
sequence Q
description BINDING SITE FOR RESIDUE ACT A 1550
source : AC3

34) chain B
residue 119
type
sequence K
description BINDING SITE FOR RESIDUE ACT B 1540
source : AC4

35) chain B
residue 146
type
sequence T
description BINDING SITE FOR RESIDUE ACT B 1540
source : AC4

36) chain B
residue 147
type
sequence S
description BINDING SITE FOR RESIDUE ACT B 1540
source : AC4

37) chain B
residue 149
type
sequence N
description BINDING SITE FOR RESIDUE ACT B 1540
source : AC4

38) chain B
residue 150
type
sequence T
description BINDING SITE FOR RESIDUE ACT B 1540
source : AC4

39) chain B
residue 222
type
sequence Q
description BINDING SITE FOR RESIDUE ACT B 1540
source : AC4

40) chain B
residue 187
type
sequence E
description BINDING SITE FOR RESIDUE ACT B 1541
source : AC5

41) chain B
residue 189
type
sequence V
description BINDING SITE FOR RESIDUE ACT B 1541
source : AC5

42) chain B
residue 409
type
sequence W
description BINDING SITE FOR RESIDUE ACT B 1542
source : AC6

43) chain B
residue 530
type
sequence L
description BINDING SITE FOR RESIDUE ACT B 1542
source : AC6

44) chain A
residue 119
type
sequence K
description BINDING SITE FOR RESIDUE PLP A 1551
source : AC7

45) chain A
residue 149
type
sequence N
description BINDING SITE FOR RESIDUE PLP A 1551
source : AC7

46) chain A
residue 254
type
sequence S
description BINDING SITE FOR RESIDUE PLP A 1551
source : AC7

47) chain A
residue 255
type
sequence V
description BINDING SITE FOR RESIDUE PLP A 1551
source : AC7

48) chain A
residue 256
type
sequence G
description BINDING SITE FOR RESIDUE PLP A 1551
source : AC7

49) chain A
residue 257
type
sequence T
description BINDING SITE FOR RESIDUE PLP A 1551
source : AC7

50) chain A
residue 258
type
sequence G
description BINDING SITE FOR RESIDUE PLP A 1551
source : AC7

51) chain A
residue 259
type
sequence G
description BINDING SITE FOR RESIDUE PLP A 1551
source : AC7

52) chain A
residue 260
type
sequence T
description BINDING SITE FOR RESIDUE PLP A 1551
source : AC7

53) chain A
residue 305
type
sequence G
description BINDING SITE FOR RESIDUE PLP A 1551
source : AC7

54) chain A
residue 306
type
sequence I
description BINDING SITE FOR RESIDUE PLP A 1551
source : AC7

55) chain A
residue 349
type
sequence S
description BINDING SITE FOR RESIDUE PLP A 1551
source : AC7

56) chain A
residue 375
type
sequence P
description BINDING SITE FOR RESIDUE PLP A 1551
source : AC7

57) chain A
residue 376
type
sequence D
description BINDING SITE FOR RESIDUE PLP A 1551
source : AC7

58) chain B
residue 119
type
sequence K
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

59) chain B
residue 149
type
sequence N
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

60) chain B
residue 254
type
sequence S
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

61) chain B
residue 255
type
sequence V
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

62) chain B
residue 256
type
sequence G
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

63) chain B
residue 257
type
sequence T
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

64) chain B
residue 258
type
sequence G
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

65) chain B
residue 259
type
sequence G
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

66) chain B
residue 260
type
sequence T
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

67) chain B
residue 304
type
sequence E
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

68) chain B
residue 305
type
sequence G
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

69) chain B
residue 306
type
sequence I
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

70) chain B
residue 349
type
sequence S
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

71) chain B
residue 375
type
sequence P
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

72) chain B
residue 376
type
sequence D
description BINDING SITE FOR RESIDUE PLP B 1543
source : AC8

73) chain A
residue 50
type
sequence S
description BINDING SITE FOR RESIDUE EDO A 1552
source : AC9

74) chain A
residue 229
type
sequence P
description BINDING SITE FOR RESIDUE EDO A 1552
source : AC9

75) chain A
residue 262
type
sequence T
description BINDING SITE FOR RESIDUE EDO A 1552
source : AC9

76) chain A
residue 266
type
sequence R
description BINDING SITE FOR RESIDUE EDO A 1552
source : AC9

77) chain A
residue 313
type
sequence T
description BINDING SITE FOR RESIDUE EDO A 1552
source : AC9

78) chain A
residue 314
type
sequence V
description BINDING SITE FOR RESIDUE EDO A 1552
source : AC9

79) chain A
residue 195
type
sequence A
description BINDING SITE FOR RESIDUE EDO A 1553
source : BC1

80) chain A
residue 197
type
sequence F
description BINDING SITE FOR RESIDUE EDO A 1553
source : BC1

81) chain A
residue 202
type
sequence S
description BINDING SITE FOR RESIDUE EDO A 1553
source : BC1

82) chain A
residue 203
type
sequence H
description BINDING SITE FOR RESIDUE EDO A 1553
source : BC1

83) chain A
residue 308
type
sequence Y
description BINDING SITE FOR RESIDUE EDO A 1553
source : BC1

84) chain A
residue 309
type
sequence D
description BINDING SITE FOR RESIDUE EDO A 1553
source : BC1

85) chain B
residue 50
type
sequence S
description BINDING SITE FOR RESIDUE EDO B 1544
source : BC2

86) chain B
residue 262
type
sequence T
description BINDING SITE FOR RESIDUE EDO B 1544
source : BC2

87) chain B
residue 266
type
sequence R
description BINDING SITE FOR RESIDUE EDO B 1544
source : BC2

88) chain B
residue 313
type
sequence T
description BINDING SITE FOR RESIDUE EDO B 1544
source : BC2

89) chain B
residue 314
type
sequence V
description BINDING SITE FOR RESIDUE EDO B 1544
source : BC2

90) chain A
residue 187
type
sequence E
description BINDING SITE FOR RESIDUE EDO A 1554
source : BC3

91) chain A
residue 485
type
sequence K
description BINDING SITE FOR RESIDUE EDO A 1555
source : BC4

92) chain A
residue 486
type
sequence Q
description BINDING SITE FOR RESIDUE EDO A 1555
source : BC4

93) chain A
residue 487
type
sequence F
description BINDING SITE FOR RESIDUE EDO A 1555
source : BC4

94) chain A
residue 315
type
sequence L
description BINDING SITE FOR RESIDUE EDO A 1556
source : BC5

95) chain A
residue 316
type
sequence D
description BINDING SITE FOR RESIDUE EDO A 1556
source : BC5

96) chain A
residue 317
type
sequence R
description BINDING SITE FOR RESIDUE EDO A 1556
source : BC5

97) chain A
residue 198
type
sequence D
description BINDING SITE FOR RESIDUE PE4 A 1557
source : BC6

98) chain A
residue 200
type
sequence P
description BINDING SITE FOR RESIDUE PE4 A 1557
source : BC6

99) chain A
residue 436
type
sequence E
description BINDING SITE FOR RESIDUE PE4 A 1557
source : BC6

100) chain A
residue 439
type
sequence R
description BINDING SITE FOR RESIDUE PE4 A 1557
source : BC6

101) chain B
residue 462
type
sequence G
description BINDING SITE FOR RESIDUE PE4 A 1557
source : BC6

102) chain A
residue 172
type
sequence K
description BINDING SITE FOR RESIDUE NA A 1558
source : BC7

103) chain A
residue 173
type
sequence M
description BINDING SITE FOR RESIDUE NA A 1558
source : BC7

104) chain A
residue 305
type
sequence G
description BINDING SITE FOR RESIDUE NA A 1558
source : BC7

105) chain A
residue 306
type
sequence I
description BINDING SITE FOR RESIDUE NA A 1558
source : BC7

106) chain B
residue 172
type
sequence K
description BINDING SITE FOR RESIDUE NA B 1545
source : BC8

107) chain B
residue 173
type
sequence M
description BINDING SITE FOR RESIDUE NA B 1545
source : BC8

108) chain B
residue 305
type
sequence G
description BINDING SITE FOR RESIDUE NA B 1545
source : BC8

109) chain B
residue 306
type
sequence I
description BINDING SITE FOR RESIDUE NA B 1545
source : BC8

110) chain A
residue 188
type
sequence I
description BINDING SITE FOR RESIDUE ACT B 1546
source : BC9

111) chain A
residue 189
type
sequence V
description BINDING SITE FOR RESIDUE ACT B 1546
source : BC9

112) chain B
residue 500
type
sequence S
description BINDING SITE FOR RESIDUE ACT B 1546
source : BC9

113) chain B
residue 504
type
sequence E
description BINDING SITE FOR RESIDUE ACT B 1546
source : BC9

114) chain B
residue 529
type
sequence L
description BINDING SITE FOR RESIDUE ACT B 1546
source : BC9

115) chain A
residue 539
type
sequence L
description BINDING SITE FOR RESIDUE EDO A 1559
source : CC1

116) chain A
residue 540
type
sequence L
description BINDING SITE FOR RESIDUE EDO A 1559
source : CC1

117) chain A
residue 119
type catalytic
sequence K
description 713
source MCSA : MCSA1

118) chain B
residue 119
type catalytic
sequence K
description 713
source MCSA : MCSA2

119) chain A
residue 108-126
type prosite
sequence KCEFFNAGGSVKDRISLRM
description CYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KcEffn.AGgSVKdRiSlrM
source prosite : PS00901

120) chain A
residue 52
type BINDING
sequence C
description axial binding residue => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
source Swiss-Prot : SWS_FT_FI1

121) chain A
residue 65
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
source Swiss-Prot : SWS_FT_FI1

122) chain B
residue 52
type BINDING
sequence C
description axial binding residue => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
source Swiss-Prot : SWS_FT_FI1

123) chain B
residue 65
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
source Swiss-Prot : SWS_FT_FI1

124) chain A
residue 149
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
source Swiss-Prot : SWS_FT_FI2

125) chain A
residue 256
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
source Swiss-Prot : SWS_FT_FI2

126) chain A
residue 349
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
source Swiss-Prot : SWS_FT_FI2

127) chain B
residue 149
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
source Swiss-Prot : SWS_FT_FI2

128) chain B
residue 256
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
source Swiss-Prot : SWS_FT_FI2

129) chain B
residue 349
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
source Swiss-Prot : SWS_FT_FI2

130) chain A
residue 119
type MOD_RES
sequence K
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
source Swiss-Prot : SWS_FT_FI4

131) chain B
residue 119
type MOD_RES
sequence K
description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11483494, ECO:0000269|PubMed:12173932
source Swiss-Prot : SWS_FT_FI4

132) chain A
residue 199
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI5

133) chain B
residue 199
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI5

134) chain A
residue 211
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:17087506
source Swiss-Prot : SWS_FT_FI6

135) chain B
residue 211
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:17087506
source Swiss-Prot : SWS_FT_FI6


Display surface

Download
Links