eF-site ID 2mvw_13-AB
PDB Code 2mvw
Model 13
Chain A, B

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Title Solution structure of the TRIM19 B-box1 (B1) of human promyelocytic leukemia (PML)
Classification METAL BINDING PROTEIN
Compound Protein PML
Source Homo sapiens (Human) (PML_HUMAN)
Sequence A:  GSRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQW
FLKHEARPLAE
B:  GSRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQW
FLKHEARPLAE
Description


Functional site

1) chain A
residue 129
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 201
source : AC1

2) chain A
residue 132
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 201
source : AC1

3) chain A
residue 148
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 201
source : AC1

4) chain A
residue 151
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 201
source : AC1

5) chain A
residue 140
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 202
source : AC2

6) chain A
residue 143
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 202
source : AC2

7) chain A
residue 155
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 202
source : AC2

8) chain A
residue 161
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 202
source : AC2

9) chain B
residue 129
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 201
source : AC3

10) chain B
residue 132
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 201
source : AC3

11) chain B
residue 148
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 201
source : AC3

12) chain B
residue 151
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 201
source : AC3

13) chain B
residue 140
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 202
source : AC4

14) chain B
residue 143
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 202
source : AC4

15) chain B
residue 155
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 202
source : AC4

16) chain B
residue 161
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 202
source : AC4

17) chain A
residue 124-166
type ZN_FING
sequence DAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEA
RPL
description B box-type 1; atypical => ECO:0000255|PROSITE-ProRule:PRU00024
source Swiss-Prot : SWS_FT_FI1

18) chain B
residue 124-166
type ZN_FING
sequence DAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEA
RPL
description B box-type 1; atypical => ECO:0000255|PROSITE-ProRule:PRU00024
source Swiss-Prot : SWS_FT_FI1

19) chain A
residue 160
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI3

20) chain B
residue 160
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI3

21) chain A
residue 129
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024
source Swiss-Prot : SWS_FT_FI2

22) chain A
residue 132
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024
source Swiss-Prot : SWS_FT_FI2

23) chain A
residue 151
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024
source Swiss-Prot : SWS_FT_FI2

24) chain A
residue 155
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024
source Swiss-Prot : SWS_FT_FI2

25) chain B
residue 129
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024
source Swiss-Prot : SWS_FT_FI2

26) chain B
residue 132
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024
source Swiss-Prot : SWS_FT_FI2

27) chain B
residue 151
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024
source Swiss-Prot : SWS_FT_FI2

28) chain B
residue 155
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00024
source Swiss-Prot : SWS_FT_FI2


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