|
eF-site ID
|
2wpk-S |
PDB Code
|
2wpk |
Chain
|
S |
|
click to enlarge
|
|
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
|
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 |
53-58 |
type |
prosite |
sequence |
VTAAHC
|
description |
TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC
|
source |
prosite : PS00134
|
|
13)
|
chain |
S |
residue |
189-200 |
type |
prosite |
sequence |
DSCQGDSGGPHV
|
description |
TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPHV
|
source |
prosite : PS00135
|
|
14)
|
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
|
|
15)
|
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
|
|
16)
|
chain |
S |
residue |
102 |
type |
ACT_SITE |
sequence |
D
|
description |
Charge relay system => ECO:0000269|PubMed:659613
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
17)
|
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
|
|
18)
|
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
|
|
19)
|
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
|
|
20)
|
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
|
|
21)
|
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
|
|
|
|