eF-site ID 6g5f-A
PDB Code 6g5f
Chain A

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Title Crystal structure of an engineered Botulinum Neurotoxin type B mutant E1191M/S1199Y in complex with human synaptotagmin 1
Classification TOXIN
Compound Botulinum neurotoxin type B
Source (SYT1_HUMAN)
Sequence A:  PVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITD
RIWIIPERYTFGYKPEDFNKSSGIFNRDVCEYYDPDYLNT
NDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGD
RRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIF
GPGPVLNENETIDIGIQNHFASREGFGGIMQMKFCPEYVS
VFNNVQENKGASIFNRRGYFSDPALILMHQLIYVLHGLYG
IKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIIT
PSTDKSIYDKVLQNFRGIVDRLNKVLVCISDPNININIYK
NKFKDKYKFVEDSEGKYSIDVESFDKLYKSLMFGFTETNI
AENYKIKTRASYFSDSLPPVKIKNLLDNEIYTIEEGFNIS
DKDMEKEYRGQNKAINKQAYEEISKEHLAVYKIQMCKSVK
Description


Functional site

1) chain A
residue 69
type
sequence D
description binding site for residue GOL A 1301
source : AC1

2) chain A
residue 259
type
sequence Q
description binding site for residue GOL A 1301
source : AC1

3) chain A
residue 375
type
sequence S
description binding site for residue GOL A 1301
source : AC1

4) chain A
residue 207
type
sequence Q
description binding site for residue GOL A 1302
source : AC2

5) chain A
residue 275
type
sequence Q
description binding site for residue GOL A 1302
source : AC2

6) chain A
residue 123
type
sequence R
description binding site for residue GOL A 1303
source : AC3

7) chain A
residue 124
type
sequence V
description binding site for residue GOL A 1303
source : AC3

8) chain A
residue 130
type
sequence N
description binding site for residue GOL A 1303
source : AC3

9) chain A
residue 259
type
sequence Q
description binding site for residue MLI B 1301
source : AC4

10) chain A
residue 374
type
sequence F
description binding site for residue MLI B 1301
source : AC4

11) chain A
residue 376
type
sequence D
description binding site for residue MLI B 1301
source : AC4

12) chain A
residue 230
type catalytic
sequence H
description 626
source MCSA : MCSA1

13) chain A
residue 231
type catalytic
sequence Q
description 626
source MCSA : MCSA1

14) chain A
residue 234
type catalytic
sequence Y
description 626
source MCSA : MCSA1

15) chain A
residue 268
type catalytic
sequence E
description 626
source MCSA : MCSA1

16) chain A
residue 370
type catalytic
sequence R
description 626
source MCSA : MCSA1

17) chain A
residue 231
type ACT_SITE
sequence Q
description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095
source Swiss-Prot : SWS_FT_FI1

18) chain A
residue 230
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:10932256, ECO:0000305|PubMed:1429690, ECO:0007744|PDB:1EPW, ECO:0007744|PDB:1F31, ECO:0007744|PDB:2NP0
source Swiss-Prot : SWS_FT_FI2

19) chain A
residue 234
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:10932256, ECO:0000305|PubMed:1429690, ECO:0007744|PDB:1EPW, ECO:0007744|PDB:1F31, ECO:0007744|PDB:2NP0
source Swiss-Prot : SWS_FT_FI2

20) chain A
residue 268
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:10932256, ECO:0007744|PDB:1EPW, ECO:0007744|PDB:1F31, ECO:0007744|PDB:2NP0
source Swiss-Prot : SWS_FT_FI3


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