eF-site ID 6bx8-ABCDEFGH
PDB Code 6bx8
Chain A, B, C, D, E, F, G, H

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Title Human Mesotrypsin (PRSS3) Complexed with Tissue Factor Pathway Inhibitor Variant (TFPI1-KD1-K15R-I17C-I34C)
Classification HYDROLASE
Compound Trypsin-3
Source (TFPI1_HUMAN)
Sequence A:  IVGGYTCEENSLPYQVSLNSGSHFCGGSLISEQWVVSAAH
CYKTRIQVRLGEHNIKVLEGNEQFINAAKIIRHPKYNRDT
LDNDIMLIKLSSPAVINARVSTISLPTAPPAAGTECLISG
WGNTLSFGADYPDELKCLDAPVLTQAECKASYPGKITNSM
FCVGFLEGGKDSCQRDAGGPVVCNGQLQGVVSWGHGCAWK
NRPGVYTKVYNYVDWIKDTIAANS
B:  MHSFCAFKADDGPCRACMKRFFFNIFTRQCEEFCYGGCEG
NQNRFESLEECKKMC
C:  IVGGYTCEENSLPYQVSLNSGSHFCGGSLISEQWVVSAAH
CYKTRIQVRLGEHNIKVLEGNEQFINAAKIIRHPKYNRDT
LDNDIMLIKLSSPAVINARVSTISLPTAPPAAGTECLISG
WGNTLSFGADYPDELKCLDAPVLTQAECKASYPGKITNSM
FCVGFLEGGKDSCQRDAGGPVVCNGQLQGVVSWGHGCAWK
NRPGVYTKVYNYVDWIKDTIAANS
D:  SFCAFKADDGPCRACMKRFFFNIFTRQCEEFCYGGCEGNQ
NRFESLEECKKMC
E:  IVGGYTCEENSLPYQVSLNSGSHFCGGSLISEQWVVSAAH
CYKTRIQVRLGEHNIKVLEGNEQFINAAKIIRHPKYNRDT
LDNDIMLIKLSSPAVINARVSTISLPTAPPAAGTECLISG
WGNTLSFGADYPDELKCLDAPVLTQAECKASYPGKITNSM
FCVGFLEGGKDSCQRDAGGPVVCNGQLQGVVSWGHGCAWK
NRPGVYTKVYNYVDWIKDTIAANS
F:  HSFCAFKADDGPCRACMKRFFFNIFTRQCEEFCYGGCEGN
QNRFESLEECKKMC
G:  IVGGYTCEENSLPYQVSLNSGSHFCGGSLISEQWVVSAAH
CYKTRIQVRLGEHNIKVLEGNEQFINAAKIIRHPKYNRDT
LDNDIMLIKLSSPAVINARVSTISLPTAPPAAGTECLISG
WGNTLSFGADYPDELKCLDAPVLTQAECKASYPGKITNSM
FCVGFLEGGKDSCQRDAGGPVVCNGQLQGVVSWGHGCAWK
NRPGVYTKVYNYVDWIKDTIAANS
H:  MHSFCAFKADDGPCRACMKRFFFNIFTRQCEEFCYGGCEG
NQNRFESLEECKKMC
Description


Functional site
1) chain A
residue 20
type
sequence Y
description binding site for residue SO4 B 101
source : AC1
2) chain A
residue 21
type
sequence T
description binding site for residue SO4 B 101
source : AC1
3) chain B
residue 20
type
sequence R
description binding site for residue SO4 B 101
source : AC1
4) chain B
residue 44
type
sequence R
description binding site for residue SO4 B 101
source : AC1
5) chain C
residue 20
type
sequence Y
description binding site for residue SO4 C 301
source : AC2
6) chain C
residue 21
type
sequence T
description binding site for residue SO4 C 301
source : AC2
7) chain D
residue 20
type
sequence R
description binding site for residue SO4 C 301
source : AC2
8) chain D
residue 44
type
sequence R
description binding site for residue SO4 C 301
source : AC2
9) chain D
residue 46
type
sequence E
description binding site for residue SO4 C 301
source : AC2
10) chain E
residue 20
type
sequence Y
description binding site for residue SO4 F 101
source : AC3
11) chain E
residue 21
type
sequence T
description binding site for residue SO4 F 101
source : AC3
12) chain E
residue 96
type
sequence R
description binding site for residue SO4 F 101
source : AC3
13) chain F
residue 20
type
sequence R
description binding site for residue SO4 F 101
source : AC3
14) chain F
residue 44
type
sequence R
description binding site for residue SO4 F 101
source : AC3
15) chain G
residue 18
type
sequence G
description binding site for residue SO4 H 101
source : AC4
16) chain G
residue 188
type
sequence G
description binding site for residue SO4 H 101
source : AC4
17) chain H
residue 20
type
sequence R
description binding site for residue SO4 H 101
source : AC4
18) chain H
residue 35
type
sequence Y
description binding site for residue SO4 H 101
source : AC4
19) chain H
residue 44
type
sequence R
description binding site for residue SO4 H 101
source : AC4
20) chain B
residue 15
type SITE
sequence R
description Reactive bond
source Swiss-Prot : SWS_FT_FI1
21) chain G
residue 57
type SITE
sequence H
description Reactive bond
source Swiss-Prot : SWS_FT_FI1
22) chain G
residue 102
type SITE
sequence D
description Reactive bond
source Swiss-Prot : SWS_FT_FI1
23) chain G
residue 195
type SITE
sequence A
description Reactive bond
source Swiss-Prot : SWS_FT_FI1
24) chain D
residue 15
type SITE
sequence R
description Reactive bond
source Swiss-Prot : SWS_FT_FI1
25) chain F
residue 15
type SITE
sequence R
description Reactive bond
source Swiss-Prot : SWS_FT_FI1
26) chain H
residue 15
type SITE
sequence R
description Reactive bond
source Swiss-Prot : SWS_FT_FI1
27) chain C
residue 102
type SITE
sequence D
description Reactive bond
source Swiss-Prot : SWS_FT_FI1
28) chain C
residue 195
type SITE
sequence A
description Reactive bond
source Swiss-Prot : SWS_FT_FI1
29) chain E
residue 57
type SITE
sequence H
description Reactive bond
source Swiss-Prot : SWS_FT_FI1
30) chain E
residue 102
type SITE
sequence D
description Reactive bond
source Swiss-Prot : SWS_FT_FI1
31) chain E
residue 195
type SITE
sequence A
description Reactive bond
source Swiss-Prot : SWS_FT_FI1
32) chain A
residue 189
type SITE
sequence D
description Required for specificity => ECO:0000250
source Swiss-Prot : SWS_FT_FI5
33) chain C
residue 189
type SITE
sequence D
description Required for specificity => ECO:0000250
source Swiss-Prot : SWS_FT_FI5
34) chain E
residue 189
type SITE
sequence D
description Required for specificity => ECO:0000250
source Swiss-Prot : SWS_FT_FI5
35) chain G
residue 189
type SITE
sequence D
description Required for specificity => ECO:0000250
source Swiss-Prot : SWS_FT_FI5
36) chain A
residue 151
type MOD_RES
sequence Y
description Sulfotyrosine => ECO:0000250
source Swiss-Prot : SWS_FT_FI6
37) chain C
residue 151
type MOD_RES
sequence Y
description Sulfotyrosine => ECO:0000250
source Swiss-Prot : SWS_FT_FI6
38) chain E
residue 151
type MOD_RES
sequence Y
description Sulfotyrosine => ECO:0000250
source Swiss-Prot : SWS_FT_FI6
39) chain G
residue 151
type MOD_RES
sequence Y
description Sulfotyrosine => ECO:0000250
source Swiss-Prot : SWS_FT_FI6
40) chain B
residue 33-51
type prosite
sequence FCYGGCEGNQNRFESLEEC
description BPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FcyGGCegnqnrFesleeC
source prosite : PS00280
41) chain A
residue 53-58
type prosite
sequence VSAAHC
description TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
source prosite : PS00134
42) chain A
residue 70
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI2
43) chain G
residue 70
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI2
44) chain G
residue 72
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI2
45) chain G
residue 75
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI2
46) chain A
residue 72
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI2
47) chain A
residue 75
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI2
48) chain C
residue 70
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI2
49) chain C
residue 72
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI2
50) chain C
residue 75
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI2
51) chain E
residue 70
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI2
52) chain E
residue 72
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI2
53) chain E
residue 75
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI2
54) chain A
residue 77
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT
source Swiss-Prot : SWS_FT_FI3
55) chain C
residue 77
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT
source Swiss-Prot : SWS_FT_FI3
56) chain E
residue 77
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT
source Swiss-Prot : SWS_FT_FI3
57) chain G
residue 77
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U30, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT
source Swiss-Prot : SWS_FT_FI3
58) chain A
residue 80
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI4
59) chain C
residue 80
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI4
60) chain E
residue 80
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI4
61) chain G
residue 80
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11827488, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:27810896, ECO:0007744|PDB:1H4W, ECO:0007744|PDB:3L33, ECO:0007744|PDB:3L3T, ECO:0007744|PDB:3P92, ECO:0007744|PDB:3P95, ECO:0007744|PDB:4U32, ECO:0007744|PDB:5JBT, ECO:0007744|PDB:5TP0
source Swiss-Prot : SWS_FT_FI4

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