eF-site ID 1huz-BCD
PDB Code 1huz
Chain B, C, D

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Title CRYSTAL STRUCTURE OF DNA POLYMERASE COMPLEXED WITH DNA AND CR-PCP
Classification TRANSFERASE/DNA
Compound 5'-D(*AP*AP*TP*AP*GP*GP*CP*GP*TP*CP*G)-3'
Source null (1HUZ)
Sequence B:  TLNGGITDMLVELANFEKNVSQAIHKYNAYRKAASVIAKY
PHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIR
QDDTSSSINFLTRVTGIGPSAARKLVDEGIKTLEDLRKNE
DKLNHHQRIGLKYFEDFEKRIPREEMLQMQDIVLNEVKKL
DPEYIATVCGSFRRGAESSGDMDVLLTHPNFTSESSKQPK
LLHRVVEQLQKVRFITDTLSKGETKFMGVCQLPSENDENE
YPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEK
GFTINEYTIRPLGVTGVAGEPLPVDSEQDIFDYIQWRYRE
PKDRS
C:  AGGCGTCG
D:  CGACGCCT
Description


Functional site

1) chain B
residue 190
type
sequence D
description BINDING SITE FOR RESIDUE CR B 999
source : AC2

2) chain B
residue 192
type
sequence D
description BINDING SITE FOR RESIDUE CR B 999
source : AC2

3) chain D
residue 8
type
sequence T
description BINDING SITE FOR RESIDUE CR B 999
source : AC2

4) chain B
residue 149
type
sequence R
description BINDING SITE FOR RESIDUE MDN B 338
source : AC4

5) chain B
residue 179
type
sequence G
description BINDING SITE FOR RESIDUE MDN B 338
source : AC4

6) chain B
residue 180
type
sequence S
description BINDING SITE FOR RESIDUE MDN B 338
source : AC4

7) chain B
residue 183
type
sequence R
description BINDING SITE FOR RESIDUE MDN B 338
source : AC4

8) chain B
residue 188
type
sequence S
description BINDING SITE FOR RESIDUE MDN B 338
source : AC4

9) chain B
residue 189
type
sequence G
description BINDING SITE FOR RESIDUE MDN B 338
source : AC4

10) chain B
residue 190
type
sequence D
description BINDING SITE FOR RESIDUE MDN B 338
source : AC4

11) chain B
residue 192
type
sequence D
description BINDING SITE FOR RESIDUE MDN B 338
source : AC4

12) chain D
residue 8
type
sequence T
description BINDING SITE FOR RESIDUE MDN B 338
source : AC4

13) chain B
residue 83
type MOD_RES
sequence R
description Omega-N-methylarginine; by PRMT6 => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI4

14) chain B
residue 152
type MOD_RES
sequence R
description Omega-N-methylarginine; by PRMT6 => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI4

15) chain B
residue 41
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI5

16) chain B
residue 61
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI5

17) chain B
residue 81
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI5

18) chain B
residue 72
type ACT_SITE
sequence K
description Nucleophile; Schiff-base intermediate with DNA; for 5'-dRP lyase activity => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI1

19) chain B
residue 60
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI2

20) chain B
residue 62
type BINDING
sequence L
description BINDING => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI2

21) chain B
residue 65
type BINDING
sequence V
description BINDING => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI2

22) chain B
residue 101
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI2

23) chain B
residue 103
type BINDING
sequence V
description BINDING => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI2

24) chain B
residue 106
type BINDING
sequence I
description BINDING => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI2

25) chain B
residue 149
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI2

26) chain B
residue 180
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI2

27) chain B
residue 183
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI2

28) chain B
residue 189
type BINDING
sequence G
description BINDING => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI2

29) chain B
residue 190
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI2

30) chain B
residue 192
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 256
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P06746
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 72
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:Q8K409
source Swiss-Prot : SWS_FT_FI3


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