eF-site ID 1cts-A
PDB Code 1cts
Chain A

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Title CRYSTALLOGRAPHIC REFINEMENT AND ATOMIC MODELS OF TWO DIFFERENT FORMS OF CITRATE SYNTHASE AT 2.7 AND 1.7 ANGSTROMS RESOLUTION
Classification OXO-ACID-LYASE
Compound CITRATE SYNTHASE
Source Sus scrofa (Pig) (CISY_PIG)
Sequence A:  ASSTNLKDILADLIPKEQARIKTFRQQHGNTVVGQITVDM
MYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPK
AKGGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAAL
PSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAE
GIHRTKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSI
GAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEG
GNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQE
VLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGH
AVLRKTDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNV
LLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVS
RALGVLAQLIWSRALGFPLERPKSMSTDGLIKLVDSK
Description


Functional site

1) chain A
residue 238
type
sequence H
description BINDING SITE FOR RESIDUE CIT A 438
source : AC1

2) chain A
residue 242
type
sequence N
description BINDING SITE FOR RESIDUE CIT A 438
source : AC1

3) chain A
residue 274
type
sequence H
description BINDING SITE FOR RESIDUE CIT A 438
source : AC1

4) chain A
residue 401
type
sequence R
description BINDING SITE FOR RESIDUE CIT A 438
source : AC1

5) chain A
residue 317-329
type prosite
sequence GYGHAVLRKTDPR
description CITRATE_SYNTHASE Citrate synthase signature. GYGHaVl.RktDPR
source prosite : PS00480

6) chain A
residue 274
type ACT_SITE
sequence H
description
source Swiss-Prot : SWS_FT_FI1

7) chain A
residue 320
type ACT_SITE
sequence H
description
source Swiss-Prot : SWS_FT_FI1

8) chain A
residue 375
type ACT_SITE
sequence D
description
source Swiss-Prot : SWS_FT_FI1

9) chain A
residue 49
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q29RK1
source Swiss-Prot : SWS_FT_FI2

10) chain A
residue 76
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CZU6
source Swiss-Prot : SWS_FT_FI3

11) chain A
residue 166
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CZU6
source Swiss-Prot : SWS_FT_FI3

12) chain A
residue 423
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CZU6
source Swiss-Prot : SWS_FT_FI3

13) chain A
residue 199
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:Q9CZU6
source Swiss-Prot : SWS_FT_FI4

14) chain A
residue 294
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CZU6
source Swiss-Prot : SWS_FT_FI5

15) chain A
residue 300
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CZU6
source Swiss-Prot : SWS_FT_FI5

16) chain A
residue 348
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CZU6
source Swiss-Prot : SWS_FT_FI5

17) chain A
residue 366
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CZU6
source Swiss-Prot : SWS_FT_FI5

18) chain A
residue 432
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CZU6
source Swiss-Prot : SWS_FT_FI5

19) chain A
residue 355
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:O75390
source Swiss-Prot : SWS_FT_FI6

20) chain A
residue 368
type MOD_RES
sequence K
description N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:7093227
source Swiss-Prot : SWS_FT_FI7


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