eF-site ID 1f8s-ABCDEFGH
PDB Code 1f8s
Chain A, B, C, D, E, F, G, H

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Title CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA, COMPLEXED WITH THREE MOLECULES OF O-AMINOBENZOATE.
Classification OXIDOREDUCTASE
Compound L-AMINO ACID OXIDASE
Source ORGANISM_COMMON: Malayan pit viper; ORGANISM_SCIENTIFIC: Calloselasma rhodostoma;
Sequence A:  NPLAECFQENDYEEFLEIARNGLKATSNPKHVVIVGAGMA
GLSAAYVLAGAGHQVTVLEASERPGGRVRTYRNEEAGWYA
NLGPMRLPEKHRIVREYIRKFDLRLNEFSQENDNAWYFIK
NIRKKVGEVKKDPGLLKYPVKPSEAGKSAGQLYEESLGKV
VEELKRTNCSYILNKYDTYSTKEYLIKEGDLSPGAVDMIG
DLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVDGMDKLP
TAMYRDIQDKVHFNAQVIKIQQNDQKVTVVYETLSKETPS
VTADYVIVCTTSRAVRLIKFNPPLLPKKAHALRSVHYRSG
TKIFLTCTTKFWEDDGIHGGKSTTDLPSRFIYYPNHNFTN
GVGVIIAYGIGDDANFFQALDFKDCADIVFNDLSLIHQLP
KKDIQSFCYPSVIQKWSLDKYAMGGITTFTPYQFQHFSDP
LTASQGRIYFAGEYTAQAHGWIDSTIKSGLRAARDVNLAS
EN
B:  NPLAECFQENDYEEFLEIARNGLKATSNPKHVVIVGAGMA
GLSAAYVLAGAGHQVTVLEASERPGGRVRTYRNEEAGWYA
NLGPMRLPEKHRIVREYIRKFDLRLNEFSQENDNAWYFIK
NIRKKVGEVKKDPGLLKYPVKPSEAGKSAGQLYEESLGKV
VEELKRTNCSYILNKYDTYSTKEYLIKEGDLSPGAVDMIG
DLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVDGMDKLP
TAMYRDIQDKVHFNAQVIKIQQNDQKVTVVYETLSKETPS
VTADYVIVCTTSRAVRLIKFNPPLLPKKAHALRSVHYRSG
TKIFLTCTTKFWEDDGIHGGKSTTDLPSRFIYYPNHNFTN
GVGVIIAYGIGDDANFFQALDFKDCADIVFNDLSLIHQLP
KKDIQSFCYPSVIQKWSLDKYAMGGITTFTPYQFQHFSDP
LTASQGRIYFAGEYTAQAHGWIDSTIKSGLRAARDVNLAS
EN
C:  NPLAECFQENDYEEFLEIARNGLKATSNPKHVVIVGAGMA
GLSAAYVLAGAGHQVTVLEASERPGGRVRTYRNEEAGWYA
NLGPMRLPEKHRIVREYIRKFDLRLNEFSQENDNAWYFIK
NIRKKVGEVKKDPGLLKYPVKPSEAGKSAGQLYEESLGKV
VEELKRTNCSYILNKYDTYSTKEYLIKEGDLSPGAVDMIG
DLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVDGMDKLP
TAMYRDIQDKVHFNAQVIKIQQNDQKVTVVYETLSKETPS
VTADYVIVCTTSRAVRLIKFNPPLLPKKAHALRSVHYRSG
TKIFLTCTTKFWEDDGIHGGKSTTDLPSRFIYYPNHNFTN
GVGVIIAYGIGDDANFFQALDFKDCADIVFNDLSLIHQLP
KKDIQSFCYPSVIQKWSLDKYAMGGITTFTPYQFQHFSDP
LTASQGRIYFAGEYTAQAHGWIDSTIKSGLRAARDVNLAS
EN
D:  NPLAECFQENDYEEFLEIARNGLKATSNPKHVVIVGAGMA
GLSAAYVLAGAGHQVTVLEASERPGGRVRTYRNEEAGWYA
NLGPMRLPEKHRIVREYIRKFDLRLNEFSQENDNAWYFIK
NIRKKVGEVKKDPGLLKYPVKPSEAGKSAGQLYEESLGKV
VEELKRTNCSYILNKYDTYSTKEYLIKEGDLSPGAVDMIG
DLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVDGMDKLP
TAMYRDIQDKVHFNAQVIKIQQNDQKVTVVYETLSKETPS
VTADYVIVCTTSRAVRLIKFNPPLLPKKAHALRSVHYRSG
TKIFLTCTTKFWEDDGIHGGKSTTDLPSRFIYYPNHNFTN
GVGVIIAYGIGDDANFFQALDFKDCADIVFNDLSLIHQLP
KKDIQSFCYPSVIQKWSLDKYAMGGITTFTPYQFQHFSDP
LTASQGRIYFAGEYTAQAHGWIDSTIKSGLRAARDVNLAS
EN
E:  NPLAECFQENDYEEFLEIARNGLKATSNPKHVVIVGAGMA
GLSAAYVLAGAGHQVTVLEASERPGGRVRTYRNEEAGWYA
NLGPMRLPEKHRIVREYIRKFDLRLNEFSQENDNAWYFIK
NIRKKVGEVKKDPGLLKYPVKPSEAGKSAGQLYEESLGKV
VEELKRTNCSYILNKYDTYSTKEYLIKEGDLSPGAVDMIG
DLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVDGMDKLP
TAMYRDIQDKVHFNAQVIKIQQNDQKVTVVYETLSKETPS
VTADYVIVCTTSRAVRLIKFNPPLLPKKAHALRSVHYRSG
TKIFLTCTTKFWEDDGIHGGKSTTDLPSRFIYYPNHNFTN
GVGVIIAYGIGDDANFFQALDFKDCADIVFNDLSLIHQLP
KKDIQSFCYPSVIQKWSLDKYAMGGITTFTPYQFQHFSDP
LTASQGRIYFAGEYTAQAHGWIDSTIKSGLRAARDVNLAS
EN
F:  NPLAECFQENDYEEFLEIARNGLKATSNPKHVVIVGAGMA
GLSAAYVLAGAGHQVTVLEASERPGGRVRTYRNEEAGWYA
NLGPMRLPEKHRIVREYIRKFDLRLNEFSQENDNAWYFIK
NIRKKVGEVKKDPGLLKYPVKPSEAGKSAGQLYEESLGKV
VEELKRTNCSYILNKYDTYSTKEYLIKEGDLSPGAVDMIG
DLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVDGMDKLP
TAMYRDIQDKVHFNAQVIKIQQNDQKVTVVYETLSKETPS
VTADYVIVCTTSRAVRLIKFNPPLLPKKAHALRSVHYRSG
TKIFLTCTTKFWEDDGIHGGKSTTDLPSRFIYYPNHNFTN
GVGVIIAYGIGDDANFFQALDFKDCADIVFNDLSLIHQLP
KKDIQSFCYPSVIQKWSLDKYAMGGITTFTPYQFQHFSDP
LTASQGRIYFAGEYTAQAHGWIDSTIKSGLRAARDVNLAS
EN
G:  NPLAECFQENDYEEFLEIARNGLKATSNPKHVVIVGAGMA
GLSAAYVLAGAGHQVTVLEASERPGGRVRTYRNEEAGWYA
NLGPMRLPEKHRIVREYIRKFDLRLNEFSQENDNAWYFIK
NIRKKVGEVKKDPGLLKYPVKPSEAGKSAGQLYEESLGKV
VEELKRTNCSYILNKYDTYSTKEYLIKEGDLSPGAVDMIG
DLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVDGMDKLP
TAMYRDIQDKVHFNAQVIKIQQNDQKVTVVYETLSKETPS
VTADYVIVCTTSRAVRLIKFNPPLLPKKAHALRSVHYRSG
TKIFLTCTTKFWEDDGIHGGKSTTDLPSRFIYYPNHNFTN
GVGVIIAYGIGDDANFFQALDFKDCADIVFNDLSLIHQLP
KKDIQSFCYPSVIQKWSLDKYAMGGITTFTPYQFQHFSDP
LTASQGRIYFAGEYTAQAHGWIDSTIKSGLRAARDVNLAS
EN
H:  NPLAECFQENDYEEFLEIARNGLKATSNPKHVVIVGAGMA
GLSAAYVLAGAGHQVTVLEASERPGGRVRTYRNEEAGWYA
NLGPMRLPEKHRIVREYIRKFDLRLNEFSQENDNAWYFIK
NIRKKVGEVKKDPGLLKYPVKPSEAGKSAGQLYEESLGKV
VEELKRTNCSYILNKYDTYSTKEYLIKEGDLSPGAVDMIG
DLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVDGMDKLP
TAMYRDIQDKVHFNAQVIKIQQNDQKVTVVYETLSKETPS
VTADYVIVCTTSRAVRLIKFNPPLLPKKAHALRSVHYRSG
TKIFLTCTTKFWEDDGIHGGKSTTDLPSRFIYYPNHNFTN
GVGVIIAYGIGDDANFFQALDFKDCADIVFNDLSLIHQLP
KKDIQSFCYPSVIQKWSLDKYAMGGITTFTPYQFQHFSDP
LTASQGRIYFAGEYTAQAHGWIDSTIKSGLRAARDVNLAS
EN
Description


Functional site
1) chain A
residue 223
type catalytic
sequence H
description 555
source MCSA : MCSA1
2) chain A
residue 326
type catalytic
sequence K
description 555
source MCSA : MCSA1
3) chain B
residue 223
type catalytic
sequence H
description 555
source MCSA : MCSA2
4) chain B
residue 326
type catalytic
sequence K
description 555
source MCSA : MCSA2
5) chain C
residue 223
type catalytic
sequence H
description 555
source MCSA : MCSA3
6) chain C
residue 326
type catalytic
sequence K
description 555
source MCSA : MCSA3
7) chain D
residue 223
type catalytic
sequence H
description 555
source MCSA : MCSA4
8) chain D
residue 326
type catalytic
sequence K
description 555
source MCSA : MCSA4
9) chain E
residue 223
type catalytic
sequence H
description 555
source MCSA : MCSA5
10) chain E
residue 326
type catalytic
sequence K
description 555
source MCSA : MCSA5
11) chain F
residue 223
type catalytic
sequence H
description 555
source MCSA : MCSA6
12) chain F
residue 326
type catalytic
sequence K
description 555
source MCSA : MCSA6
13) chain G
residue 223
type catalytic
sequence H
description 555
source MCSA : MCSA7
14) chain G
residue 326
type catalytic
sequence K
description 555
source MCSA : MCSA7
15) chain H
residue 223
type catalytic
sequence H
description 555
source MCSA : MCSA8
16) chain H
residue 326
type catalytic
sequence K
description 555
source MCSA : MCSA8
17) chain F
residue 71
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
18) chain F
residue 87
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
19) chain F
residue 261
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
20) chain F
residue 457
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
21) chain G
residue 43
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
22) chain G
residue 63
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
23) chain G
residue 71
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
24) chain G
residue 87
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
25) chain G
residue 261
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
26) chain G
residue 457
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
27) chain H
residue 43
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
28) chain H
residue 63
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
29) chain H
residue 71
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
30) chain H
residue 87
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
31) chain H
residue 261
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
32) chain H
residue 457
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
33) chain A
residue 43
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
34) chain B
residue 87
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
35) chain B
residue 261
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
36) chain B
residue 457
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
37) chain C
residue 43
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
38) chain C
residue 63
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
39) chain C
residue 71
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
40) chain C
residue 87
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
41) chain C
residue 261
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
42) chain C
residue 457
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
43) chain D
residue 43
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
44) chain A
residue 63
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
45) chain D
residue 63
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
46) chain D
residue 71
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
47) chain D
residue 87
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
48) chain D
residue 261
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
49) chain D
residue 457
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
50) chain E
residue 43
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
51) chain E
residue 63
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
52) chain E
residue 71
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
53) chain E
residue 87
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
54) chain E
residue 261
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
55) chain A
residue 71
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
56) chain E
residue 457
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
57) chain F
residue 43
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
58) chain F
residue 63
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
59) chain A
residue 87
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
60) chain A
residue 261
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
61) chain A
residue 457
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
62) chain B
residue 43
type BINDING
sequence M
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
63) chain B
residue 63
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
64) chain B
residue 71
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:17046020
source Swiss-Prot : SWS_FT_FI1
65) chain D
residue 372
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
66) chain F
residue 223
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
67) chain F
residue 372
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
68) chain G
residue 90
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
69) chain G
residue 223
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
70) chain G
residue 372
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
71) chain H
residue 90
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
72) chain H
residue 223
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
73) chain H
residue 372
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
74) chain D
residue 90
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
75) chain D
residue 223
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
76) chain E
residue 90
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
77) chain E
residue 223
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
78) chain E
residue 372
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
79) chain F
residue 90
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
80) chain A
residue 372
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
81) chain B
residue 90
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
82) chain B
residue 223
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
83) chain B
residue 372
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
84) chain C
residue 90
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
85) chain C
residue 223
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
86) chain C
residue 372
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
87) chain A
residue 90
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
88) chain A
residue 223
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8R, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI2
89) chain B
residue 464
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI3
90) chain C
residue 464
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI3
91) chain D
residue 464
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI3
92) chain E
residue 464
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI3
93) chain F
residue 464
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI3
94) chain G
residue 464
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI3
95) chain H
residue 464
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI3
96) chain A
residue 464
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17046020, ECO:0007744|PDB:1F8S, ECO:0007744|PDB:2IID
source Swiss-Prot : SWS_FT_FI3
97) chain E
residue 361
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
98) chain F
residue 172
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
99) chain F
residue 361
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
100) chain G
residue 172
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
101) chain G
residue 361
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
102) chain H
residue 172
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
103) chain H
residue 361
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
104) chain E
residue 172
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
105) chain B
residue 172
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
106) chain B
residue 361
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
107) chain C
residue 172
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
108) chain C
residue 361
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
109) chain D
residue 172
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
110) chain D
residue 361
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
111) chain A
residue 172
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4
112) chain A
residue 361
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:10944103, ECO:0000269|PubMed:11453999
source Swiss-Prot : SWS_FT_FI4

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