eF-site ID 1nu9-ACDF
PDB Code 1nu9
Chain A, C, D, F

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Title Staphylocoagulase-Prethrombin-2 complex
Classification HYDROLASE/HYDROLASE INHIBITOR
Compound Thrombin light and heavy chains
Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence A:  GEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAE
IGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYP
PWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHP
RYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAAS
LLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIV
ERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGP
FVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKK
WIQKVIDQFG
C:  IVTKDYSKESRVNENSKYGTLISDWYLKGRLTSLESQFIN
ALGILETYHYGEKEYKDAKDKLMTRILGEDQYLLERKKVQ
YEEYKKLYKKYKEENPTSKVKMKTFDQYTIEDLTMREYNE
LTESLKSAVKDFEKDVEIIENQHHDLKPFTDEMEEKATAR
VDDLANKAYSVYFAFVRDTQHKTEALELKAKVDLVLGDED
KPHRISNERIEKEMIKDLESIIEDFFIETGLNKPDNITSY
DSSKHHYKNHSEGFEALVKETREAVTNANDSWKTKTVKKY
G
D:  GEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAE
IGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYP
PWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHP
RYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAAS
LLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIV
ERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGP
FVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKK
WIQKVIDQFG
F:  IVTKDYSKESRVNENSKYGTLISDWYLKGRLTSLESQFIN
ALGILETYHYGEKEYKDAKDKLMTRILGEDQYLLERKKVQ
YEEYKKLYKKYKEENPTSKVKMKTFDQYTIEDLTMREYNE
LTESLKSAVKDFEKDVEIIENQHHDLKPFTDEMEEKATAR
VDDLANKAYSVYFAFVRDTQHKTEALELKAKVDLVLGDED
KPHRISNERIEKEMIKDLESIIEDFFIETGLNKPDNITSY
DSSKHHYKNHSEGFEALVKETREAVTNANDSWKTKTVKKY
G
Description (1)  Thrombin light and heavy chains (E.C.3.4.21.5)/Staphylocoagulase


Functional site

1) chain A
residue 57
type
sequence H
description BINDING SITE FOR RESIDUE 0ZJ A 299
source : AC1

2) chain A
residue 60
type
sequence L
description BINDING SITE FOR RESIDUE 0ZJ A 299
source : AC1

3) chain A
residue 60
type
sequence L
description BINDING SITE FOR RESIDUE 0ZJ A 299
source : AC1

4) chain A
residue 99
type
sequence L
description BINDING SITE FOR RESIDUE 0ZJ A 299
source : AC1

5) chain A
residue 174
type
sequence I
description BINDING SITE FOR RESIDUE 0ZJ A 299
source : AC1

6) chain A
residue 189
type
sequence D
description BINDING SITE FOR RESIDUE 0ZJ A 299
source : AC1

7) chain A
residue 190
type
sequence A
description BINDING SITE FOR RESIDUE 0ZJ A 299
source : AC1

8) chain A
residue 193
type
sequence G
description BINDING SITE FOR RESIDUE 0ZJ A 299
source : AC1

9) chain A
residue 195
type
sequence S
description BINDING SITE FOR RESIDUE 0ZJ A 299
source : AC1

10) chain A
residue 214
type
sequence S
description BINDING SITE FOR RESIDUE 0ZJ A 299
source : AC1

11) chain A
residue 215
type
sequence W
description BINDING SITE FOR RESIDUE 0ZJ A 299
source : AC1

12) chain A
residue 216
type
sequence G
description BINDING SITE FOR RESIDUE 0ZJ A 299
source : AC1

13) chain A
residue 219
type
sequence G
description BINDING SITE FOR RESIDUE 0ZJ A 299
source : AC1

14) chain A
residue 226
type
sequence G
description BINDING SITE FOR RESIDUE 0ZJ A 299
source : AC1

15) chain D
residue 57
type
sequence H
description BINDING SITE FOR RESIDUE 0ZJ D 299
source : AC2

16) chain D
residue 60
type
sequence L
description BINDING SITE FOR RESIDUE 0ZJ D 299
source : AC2

17) chain D
residue 99
type
sequence L
description BINDING SITE FOR RESIDUE 0ZJ D 299
source : AC2

18) chain D
residue 189
type
sequence D
description BINDING SITE FOR RESIDUE 0ZJ D 299
source : AC2

19) chain D
residue 190
type
sequence A
description BINDING SITE FOR RESIDUE 0ZJ D 299
source : AC2

20) chain D
residue 193
type
sequence G
description BINDING SITE FOR RESIDUE 0ZJ D 299
source : AC2

21) chain D
residue 194
type
sequence D
description BINDING SITE FOR RESIDUE 0ZJ D 299
source : AC2

22) chain D
residue 195
type
sequence S
description BINDING SITE FOR RESIDUE 0ZJ D 299
source : AC2

23) chain D
residue 214
type
sequence S
description BINDING SITE FOR RESIDUE 0ZJ D 299
source : AC2

24) chain D
residue 215
type
sequence W
description BINDING SITE FOR RESIDUE 0ZJ D 299
source : AC2

25) chain D
residue 216
type
sequence G
description BINDING SITE FOR RESIDUE 0ZJ D 299
source : AC2

26) chain D
residue 219
type
sequence G
description BINDING SITE FOR RESIDUE 0ZJ D 299
source : AC2

27) chain D
residue 226
type
sequence G
description BINDING SITE FOR RESIDUE 0ZJ D 299
source : AC2

28) chain F
residue 106
type
sequence D
description BINDING SITE FOR RESIDUE HG F 998
source : AC3

29) chain C
residue 106
type
sequence D
description BINDING SITE FOR RESIDUE HG C 999
source : AC4

30) chain F
residue 106
type
sequence D
description BINDING SITE FOR RESIDUE HG F 997
source : AC5

31) chain C
residue 106
type
sequence D
description BINDING SITE FOR RESIDUE HG C 996
source : AC6

32) chain F
residue 84
type
sequence Y
description BINDING SITE FOR RESIDUE IMD F 2000
source : AC7

33) chain F
residue 103
type
sequence K
description BINDING SITE FOR RESIDUE IMD F 2000
source : AC7

34) chain C
residue 84
type
sequence Y
description BINDING SITE FOR RESIDUE IMD C 2001
source : AC8

35) chain C
residue 103
type
sequence K
description BINDING SITE FOR RESIDUE IMD C 2001
source : AC8

36) chain F
residue 247
type
sequence Y
description BINDING SITE FOR RESIDUE IMD F 2002
source : AC9

37) chain C
residue 233
type
sequence K
description BINDING SITE FOR RESIDUE IMD C 2003
source : BC1

38) chain C
residue 234
type
sequence P
description BINDING SITE FOR RESIDUE IMD C 2003
source : BC1

39) chain C
residue 235
type
sequence D
description BINDING SITE FOR RESIDUE IMD C 2003
source : BC1

40) chain F
residue 233
type
sequence K
description BINDING SITE FOR RESIDUE IMD F 2004
source : BC2

41) chain F
residue 234
type
sequence P
description BINDING SITE FOR RESIDUE IMD F 2004
source : BC2

42) chain A
residue 53-58
type prosite
sequence LTAAHC
description TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
source prosite : PS00134

43) chain A
residue 189-200
type prosite
sequence DACEGDSGGPFV
description TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
source prosite : PS00135

44) chain A
residue 57
type ACT_SITE
sequence H
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

45) chain A
residue 102
type ACT_SITE
sequence D
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

46) chain A
residue 195
type ACT_SITE
sequence S
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

47) chain D
residue 57
type ACT_SITE
sequence H
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

48) chain D
residue 102
type ACT_SITE
sequence D
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

49) chain D
residue 195
type ACT_SITE
sequence S
description Charge relay system
source Swiss-Prot : SWS_FT_FI1

50) chain A
residue 15
type SITE
sequence R
description Cleavage; by factor Xa => ECO:0000269|PubMed:34265300
source Swiss-Prot : SWS_FT_FI2

51) chain D
residue 15
type SITE
sequence R
description Cleavage; by factor Xa => ECO:0000269|PubMed:34265300
source Swiss-Prot : SWS_FT_FI2

52) chain A
residue 60
type CARBOHYD
sequence L
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923
source Swiss-Prot : SWS_FT_FI3

53) chain D
residue 60
type CARBOHYD
sequence L
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923
source Swiss-Prot : SWS_FT_FI3


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