eF-site ID 4coo-B
PDB Code 4coo
Chain B

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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 B:  WIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILK
KIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRI
SLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRG
YRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPES
HVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQ
QCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDP
EGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDK
WFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQ
ELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKKPWW
WHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVV
DEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQ
IRLTDTLGRLSHILEMDHFALVVHEQQMVFGVVTAIDLLN
FVAAQER
Description


Functional site

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

53) 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

54) 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

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

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

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

58) 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

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

60) 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


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