eF-site ID 5dlj-ABCDEFGH
PDB Code 5dlj
Chain A, B, C, D, E, F, G, H

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Title Crystal Structure of Cas-DNA-N1 complex
Classification HYDROLASE/DNA
Compound CRISPR-associated endonuclease Cas1
Source Escherichia coli (strain K12) (CAS2_ECOLI)
Sequence A:  VSMIFLQYGQIDVIDGAFVLIDKTGIRTHIPVGSVACIML
EPGTRVSHAAVRLAAQVGTLLVWVGEAGVRVYASGQPGGA
RSDKLLYQAKLALDEDLRLKVVRKMFELRFGEPAPARRSV
EQLRGIEGSRVRATYALLAKQYGVTWNGRRYDPKDWEKGD
TINQCISAATSCLYGVTEAAILAAGYAPAIGFVHTGKPLS
FVYDIADIIKFDTVVPKAFEIARRNPGEPDREVRLACRDI
FRSSKTLAKLIPLIEDVLAAGEIQPPA
B:  TWLPLNPIPLKDRVSMIFLQYGQIDVIDGAFVLIDKTGIR
THIPVGSVACIMLEPGTRVSHAAVRLAAQVGTLLVWVGEA
GVRVYASGQPGGARSDKLLYQAKLALDEDLRLKVVRKMFE
LRFGEPAPARRSVEQLRGIEGSRVRATYALLAKQYGVTWN
GRRYDPKDWEKGDTINQCISAATSCLYGVTEAAILAAGYA
PAIGFVHTGKPLSFVYDIADIIKFDTVVPKAFEIARRNPG
EPDREVRLACRDIFRSSKTLAKLIPLIEDVLAAGEIQPPA
C:  TWLPLNPIPLKDRVSMIFLQYGQIDVIDGAFVLIDKTGIR
THIPVGSVACIMLEPGTRVSHAAVRLAAQVGTLLVWVGEA
GVRVYASGQPGGARSDKLLYQAKLALDEDLRLKVVRKMFE
LRFGEPAPARRSVEQLRGIEGSRVRATYALLAKQYGVTWN
GRRYDPKDWEKGDTINQCISAATSCLYGVTEAAILAAGYA
PAIGFVHTGKPLSFVYDIADIIKFDTVVPKAFEIARRNPG
EPDREVRLACRDIFRSSKTLAKLIPLIEDVLAAGEIQPPA
D:  VSMIFLQYGQIDVIDGAFVLIDKTGIRTHIPVGSVACIML
EPGTRVSHAAVRLAAQVGTLLVWVGEAGVRVYASGQPGGA
RSDKLLYQAKLALDEDLRLKVVRKMFELRFGEPAPARRSV
EQLRGIEGSRVRATYALLAKQYGVTWNGRRYDPKDWEKGD
TINQCISAATSCLYGVTEAAILAAGYAPAIGFVHTGKPLS
FVYDIADIIKFDTVVPKAFEIARRNPGEPDREVRLACRDI
FRSSKTLAKLIPLIEDVLAAGEIQPPA
E:  MSMLVVVTENVPPRLRGRLAIWLLEVRAGVYVGDVSAKIR
EMIWEQIAGLAEEGNVVMAWATNTETGFEFQTFGLNRR
F:  MSMLVVVTENVPPRLRGRLAIWLLEVRAGVYVGDVSAKIR
EMIWEQIAGLAEEGNVVMAWATNTETGFEFQTFGLNRR
G:  TTTTTTCGTAGCTGAGGGCCTCAGCTACGTTTTTTTTTT
H:  TTTTTTCGTAGCTGAGGCCCTCAGCTACGTTTTTTTTTT
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 D
residue 221
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:26503043, ECO:0007744|PDB:5DS5
source Swiss-Prot : SWS_FT_FI1

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

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

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

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

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

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

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

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

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


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