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