eF-site ID 5dqt-ABCDEFIJKLMN
PDB Code 5dqt
Chain A, B, C, D, E, F, I, J, K, L, M, N

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Title Crystal Structure of Cas-DNA-22 complex
Classification HYDROLASE/DNA
Compound CRISPR-associated endonuclease Cas1
Source Escherichia coli (strain K12) (5DQT)
Sequence A:  VSMIFLQYGQIDVIDGAFVLIDKTGIRTHIPVGSVACIML
EPGTRVSHAAVRLAAQVGTLLVWVGEAGVRVYASGQPGGA
RSDKLLYQAKLALDEDLRLKVVRKMFELRFGEPAPARRSV
EQLRGIEGSRVRATYALLAKQYGVTWNGRRYDPKDWEKGD
TINQCISAATSCLYGVTEAAILAAGYAPAIGFVHTGKPLS
FVYDIADIIKFDTVVPKAFEIARRNPGEPDREVRLACRDI
FRSSKTLAKLIPLIEDVLAAGEIQPPA
B:  TWLPLNPIPLKDRVSMIFLQGQIDVIDGAFVLIDKTGIRT
HIPVGSVACIMLEPGTRVSHAAVRLAAQVGTLLVWVGEAG
VRVYASGQPGGARSDKLLYQAKLALDEDLRLKVVRKMFEL
RFGEPAPARRSVEQLRGIEGSRVRATYALLAKQYGVTWNG
RRYDPKDWEKGDTINQCISAATSCLYGVTEAAILAAGYAP
AIGFVHTGKPLSFVYDIADIIKFDTVVPKAFEIARRNPGE
PDREVRLACRDIFRSSKTLAKLIPLIEDVLAAGEIQPPA
C:  TWLPLNPIPLKDRVSMIFLQYGQIDVIDGAFVLIDKTGIR
THIPVGSVACIMLEPGTRVSHAAVRLAAQVGTLLVWVGEA
GVRVYASGQPGGARSDKLLYQAKLALDEDLRLKVVRKMFE
LRFGEPAPARRSVEQLRGIEGSRVRATYALLAKQYGVTWN
GRRYDPKDWEKGDTINQCISAATSCLYGVTEAAILAAGYA
PAIGFVHTGKPLSFVYDIADIIKFDTVVPKAFEIARRNPG
EPDREVRLACRDIFRSSKTLAKLIPLIEDVLAAGEIQP
D:  VSMIFLQYGQIDVIDGAFVLIDKTGIRTHIPVGSVACIML
EPGTRVSHAAVRLAAQVGTLLVWVGEAGVRVYASGQPGGA
RSDKLLYQAKLALDEDLRLKVVRKMFELRFGEPAPARRSV
EQLRGIEGSRVRATYALLAKQYGVTWNEKGDTINQCISAA
TSCLYGVTEAAILAAGYAPAIGFVHTGKPLSFVYDIADII
KFDTVVPKAFEIARRNPDREVRLACRDIFRSSKTLAKLIP
LIEDVLAAGEIQPPA
E:  MSMLVVVTENVPPRLRGRLAIWLLEVRAGVYVGDVSAKIR
EMIWEQIAGLAEEGNVVMAWATNTETGFEFQTFGLNRRTP
VDLDGLRLVSFLP
F:  MSMLVVVTENVPPRLRGRLAIWLLEVRAGVYVGDVSAKIR
EMIWEQIAGLAEEGNVVMAWATNTETGFEFQTFGLNRRTP
VDLDGLRLVSFLP
I:  VSMIFLQYGQIDVIDGAFVLIDKTGIRTHIPVGSVACIML
EPGTRVSHAAVRLAAQVGTLLVWVGEAGVRVYASGQPGGA
RSDKLLYQAKLALDEDLRLKVVRKMFELRFGEPAPARRSV
EQLRGIEGSRVRATYALLAKQYGVTWNGRRYDPKDWEKGD
TINQCISAATSCLYGVTEAAILAAGYAPAIGFVHTGKPLS
FVYDIADIIKFDTVVPKAFEIARRNPGEPDREVRLACRDI
FRSSKTLAKLIPLIEDVLAAGEIQPPA
J:  TWLPLNPIPLKDRVSMIFLQYGQIDVIDGAFVLIDKTGIR
THIPVGSVACIMLEPGTRVSHAAVRLAAQVGTLLVWVGEA
GVRVYASGQPGGARSDKLLYQAKLALDEDLRLKVVRKMFE
LRFGEPAPARRSVEQLRGIEGSRVRATYALLAKQYGVTWN
GRRYDPKDWEKGDTINQCISAATSCLYGVTEAAILAAGYA
PAIGFVHTGKPLSFVYDIADIIKFDTVVPKAFEIARRNPG
EPDREVRLACRDIFRSSKTLAKLIPLIEDVLAAGEIQPPA
K:  TWLPLNPIPLKDRVSMIFLQYGQIDVIDGAFVLIDKTGIR
THIPVGSVACIMLEPGTRVSHAAVRLAAQVGTLLVWVGEA
GVRVYASGQPGGARSDKLLYQAKLALDEDLRLKVVRKMFE
LRFGEPAPARRSVEQLRGIEGSRVRATYALLAKQYGVTWN
GRRYDPKDWEKGDTINQCISAATSCLYGVTEAAILAAGYA
PAIGFVHTGKPLSFVYDIADIIKFDTVVPKAFEIARRNPG
EPDREVRLACRDIFRSSKTLAKLIPLIEDVLAAGEIQP
L:  VSMIFLQYGQIDVIDGAFVLIDKTGIRTHIPVGSVACIML
EPGTRVSHAAVRLAAQVGTLLVWVGEAGVRVYASGQPGGA
RSDKLLYQAKLALDEDLRLKVVRKMFELRFGEPAPARRSV
EQLRGIEGSRVRATYALLAKQYGVTWNGRRYDPKDWEKGD
TINQCISAATSCLYGVTEAAILAAGYAPAIGFVHTGKPLS
FVYDIADIIKFDTVVPKAFEIARRNPGEPDREVRLACRDI
FRSSKTLAKLIPLIEDVLAAGEIQPPA
M:  MSMLVVVTENVPPRLRGRLAIWLLEVRAGVYVGDVSAKIR
EMIWEQIAGLAEEGNVVMAWATNTETGFEFQTFGLNRRTP
VDLDGLRLVSFL
N:  MSMLVVVTENVPPRLRGRLAIWLLEVRAGVYVGDVSAKIR
EMIWEQIAGLAEEGNVVMAWATNTETGFEFQTFGLNRRTP
VDLDGLRLVSFL
Description


Functional site

1) chain D
residue 141
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

2) chain L
residue 221
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

3) chain K
residue 141
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

4) chain K
residue 221
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

5) chain I
residue 141
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

6) chain I
residue 221
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

7) chain J
residue 141
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

8) chain J
residue 221
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

9) chain D
residue 221
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

10) chain C
residue 141
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

11) chain C
residue 221
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 141
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 221
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

14) chain B
residue 141
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

15) chain B
residue 221
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

16) chain L
residue 141
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

17) chain D
residue 208
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:26503043
source Swiss-Prot : SWS_FT_FI2

18) chain C
residue 208
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:26503043
source Swiss-Prot : SWS_FT_FI2

19) chain A
residue 208
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:26503043
source Swiss-Prot : SWS_FT_FI2

20) chain B
residue 208
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:26503043
source Swiss-Prot : SWS_FT_FI2

21) chain L
residue 208
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:26503043
source Swiss-Prot : SWS_FT_FI2

22) chain K
residue 208
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:26503043
source Swiss-Prot : SWS_FT_FI2

23) chain I
residue 208
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:26503043
source Swiss-Prot : SWS_FT_FI2

24) chain J
residue 208
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:26503043
source Swiss-Prot : SWS_FT_FI2


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