eF-site ID 2wpk-ES
PDB Code 2wpk
Chain E, S

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Title factor IXa superactive triple mutant, ethylene glycol-soaked
Classification BLOOD CLOTTING
Compound COAGULATION FACTOR IXA LIGHT CHAIN
Source Homo sapiens (Human) (FA9_HUMAN)
Sequence E:  TCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEP
AVPFPCGRVSVSQTSKLTR
S:  VVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAA
HCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNFN
AAINTYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFL
KFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRST
KFTITNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLT
GIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
Description


Functional site

1) chain S
residue 70
type
sequence E
description BINDING SITE FOR RESIDUE CA S 1246
source : AC1

2) chain S
residue 72
type
sequence N
description BINDING SITE FOR RESIDUE CA S 1246
source : AC1

3) chain S
residue 75
type
sequence E
description BINDING SITE FOR RESIDUE CA S 1246
source : AC1

4) chain S
residue 77
type
sequence E
description BINDING SITE FOR RESIDUE CA S 1246
source : AC1

5) chain S
residue 80
type
sequence E
description BINDING SITE FOR RESIDUE CA S 1246
source : AC1

6) chain S
residue 171
type
sequence S
description BINDING SITE FOR RESIDUE EDO S 1247
source : AC2

7) chain S
residue 216
type
sequence G
description BINDING SITE FOR RESIDUE EDO S 1247
source : AC2

8) chain S
residue 217
type
sequence E
description BINDING SITE FOR RESIDUE EDO S 1247
source : AC2

9) chain S
residue 224
type
sequence K
description BINDING SITE FOR RESIDUE EDO S 1247
source : AC2

10) chain S
residue 225
type
sequence Y
description BINDING SITE FOR RESIDUE EDO S 1247
source : AC2

11) chain S
residue 227
type
sequence I
description BINDING SITE FOR RESIDUE EDO S 1247
source : AC2

12) chain S
residue 80
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10467148, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM, ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3, ECO:0007744|PDB:3LC5
source Swiss-Prot : SWS_FT_FI4

13) chain S
residue 70
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10467148, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN, ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM, ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3, ECO:0007744|PDB:3LC5
source Swiss-Prot : SWS_FT_FI3

14) chain S
residue 72
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:10467148, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN, ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM, ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3, ECO:0007744|PDB:3LC5
source Swiss-Prot : SWS_FT_FI3

15) chain S
residue 75
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10467148, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN, ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM, ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3, ECO:0007744|PDB:3LC5
source Swiss-Prot : SWS_FT_FI3

16) chain S
residue 77
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10467148, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN, ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM, ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3, ECO:0007744|PDB:3LC5
source Swiss-Prot : SWS_FT_FI3

17) chain S
residue 57
type ACT_SITE
sequence H
description Charge relay system => ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:659613
source Swiss-Prot : SWS_FT_FI1

18) chain S
residue 195
type ACT_SITE
sequence S
description Charge relay system => ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:659613
source Swiss-Prot : SWS_FT_FI1

19) chain S
residue 102
type ACT_SITE
sequence D
description Charge relay system => ECO:0000269|PubMed:659613
source Swiss-Prot : SWS_FT_FI2

20) chain E
residue 109-124
type prosite
sequence CSCTEGYRLAENQKSC
description EGF_2 EGF-like domain signature 2. CsCteGYrlaenqksC
source prosite : PS01186

21) chain S
residue 53-58
type prosite
sequence VTAAHC
description TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC
source prosite : PS00134

22) chain S
residue 189-200
type prosite
sequence DSCQGDSGGPHV
description TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPHV
source prosite : PS00135


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