eF-site ID 1ntg-ABCD
PDB Code 1ntg
Chain A, B, C, D

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Title Crystal Structure of the EMAP II-like Cytokine Released from human tyrosyl-tRNA Synthetase
Classification LIGASE
Compound Tyrosyl-tRNA synthetase
Source (SYYC_HUMAN)
Sequence A:  PEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEP
RTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGM
LLCASIEGINRQVEPLDPPAGSAPGEHVFVKGYEKGQPDE
ELKPKKKVFEKLQADFKISEECIAQWKQTNFMTKLGSISC
KSLKGGNISLE
B:  PEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEP
RTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGM
LLCASIEGINRQVEPLDPPAGSAPGEHVFVKGYEKGQPDE
ELKPKKKVFEKLQADFKISEECIAQWKQTNFMTKLGSISC
KSLKGGNISLE
C:  PEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEP
RTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGM
LLCASIEGINRQVEPLDPPAGSAPGEHVFVKGYEKGQPDE
ELKPKKKVFEKLQADFKISEECIAQWKQTNFMTKLGSISC
KSLKGGNISLE
D:  PEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEP
RTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGM
LLCASIEGINRQVEPLDPPAGSAPGEHVFVKGYEKGQPDE
ELKPKKKVFEKLQADFKISEECIAQWKQTNFMTKLGSISC
KSLKGGNISLE
Description


Functional site

1) chain A
residue 28
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI1

2) chain B
residue 28
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI1

3) chain C
residue 28
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI1

4) chain D
residue 28
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 116
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

6) chain D
residue 116
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

7) chain D
residue 124
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

8) chain D
residue 132
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

9) chain A
residue 124
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

10) chain A
residue 132
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

11) chain B
residue 116
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

12) chain B
residue 124
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

13) chain B
residue 132
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

14) chain C
residue 116
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

15) chain C
residue 124
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

16) chain C
residue 132
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2


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