eF-site ID 5dqu-ABCDEF
PDB Code 5dqu
Chain A, B, C, D, E, F

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Title Crystal Structure of Cas-DNA-10 complex
Classification HYDROLASE/DNA
Compound CRISPR-associated endonuclease Cas1
Source Escherichia coli (strain K12) (5DQU)
Sequence A:  VSMIFLQYGQIDVIDGAFVLIDKTGIRTHIPVGSVACIML
EPGTRVSHAAVRLAAQVGTLLVWVGEAGVRVYASGQPGGA
RSDKLLYQAKLALDEDLRLKVVRKMFELRFGEPAPARSVE
QLRGIEGSRVRATYALLAKQYGVTWNGRRYDPGDTINQCI
SAATSCLYGVTEAAILAAGYAPAIGFVHTGKPLSFVYDIA
DIIKFDTVVPKAFEIARRNPGEPDREVRLACRDIFRSSKT
LAKLIPLIEDVLAAGEIQPP
B:  WLPLNPIPLKDRVSMIFLQYGQIDVIDGAFVLIDKTGIRT
HIPVGSVACIMLEPGTRVSHAAVRLAAQVGTLLVWVGEAG
VRVYASGQPGGARSDKLLYQAKLALDEDLRLKVVRKMFEL
RFGEPAPARRSVEQLRGIEGSRVRATYALLAKQYGVTWNG
RRYDPDTINQCISAATSCLYGVTEAAILAAGYAPAIGFVH
TGKPLSFVYDIADIIKFDTVVPKAFEIARRNPGEPDREVR
LACRDIFRSSKTLAKLIPLIEDVLAAGEIQ
C:  WLPLNPIPLKDRVSMIFLQYGQIDVIDGAFVLIDKTGIRT
HIPVGSVACIMLEPGTRVSHAAVRLAAQVGTLLVWVGEAG
VRVYASGQPGGARSDKLLYQAKLALDEDLRLKVVRKMFEL
RFGEPAPARRSVEQLRGIEGSRVRATYALLAKQYGVTWNG
RRYDPDTINQCISAATSCLYGVTEAAILAAGYAPAIGFVH
TGKPLSFVYDIADIIKFDTVVPKAFEIARRNPGEPDREVR
LACRDIFRSSKTLAKLIPLIEDVLAAGEIQPPAP
D:  VSMIFLQYGQIDVIDGAFVLIDKTGIRTHIPVGSVACIML
EPGTRVSHAAVRLAAQVGTLLVWVGEAGVRVYASGQPGGA
RSDKLLYQAKLALDEDLRLKVVRKMFELRPAPARVEQLRG
IEGSRVRATYALLAKQYGVTWNGRRYDPGDTINQCISAAT
SCLYGVTEAAILAAGYAPAIGFVHTGKPLSFVYDIADIIK
FDTVVPKAFEIARRNPGEPDREVRLACRDIFRSSKTLAKL
IPLIEDVLAAGEIQPPAP
E:  MSMLVVVTENVPPRLRGRLAIWLLEVRAGVYVGDVSAKIR
EMIWEQIAGLAEEGNVVMAWATNTETGFEFQTFGLNRRTP
VDLDGLRLVSFLP
F:  SMLVVVTENVPPRLRGRLAIWLLEVRAGVYVGDVSAKIRE
MIWEQIAGLAEEGNVVMAWATNTETGFEFQTFGLNRRTPV
DLDGLRLVSFLP
Description


Functional site

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

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

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

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

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

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

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

11) chain C
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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