eF-site ID 3at1-C
PDB Code 3at1
Chain C

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Title CRYSTAL STRUCTURES OF PHOSPHONOACETAMIDE LIGATED T AND PHOSPHONOACETAMIDE AND MALONATE LIGATED R STATES OF ASPARTATE CARBAMOYLTRANSFERASE AT 2.8-ANGSTROMS RESOLUTION AND NEUTRAL PH
Classification TRANSFERASE (CARBAMOYL-P,ASPARTATE)
Compound ASPARTATE CARBAMOYLTRANSFERASE (T STATE), CATALYTIC CHAIN
Source Escherichia coli (strain K12) (PYRI_ECOLI)
Sequence C:  ANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLK
HKVIASCFFEASTRTRLSFQTSMHRLGASVVGFSDSANTS
LGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSG
NVPVLNAGDGSNQHPTQTLLDLFTIQQTEGRLDNLHVAMV
GDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPEYILD
MLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEY
ANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKT
PHAWYFQQAGNGIFARQALLALVLNRDLVL
Description


Functional site

1) chain C
residue 54
type
sequence R
description PCT binding site
source : PAC

2) chain C
residue 55
type
sequence T
description PCT binding site
source : PAC

3) chain C
residue 105
type
sequence R
description PCT binding site
source : PAC

4) chain C
residue 134
type
sequence H
description PCT binding site
source : PAC

5) chain C
residue 137
type
sequence Q
description PCT binding site
source : PAC

6) chain C
residue 266
type
sequence P
description PCT binding site
source : PAC

7) chain C
residue 267
type
sequence L
description PCT binding site
source : PAC

8) chain C
residue 52
type
sequence S
description BINDING SITE FOR RESIDUE PCT C 311
source : AC4

9) chain C
residue 54
type
sequence R
description BINDING SITE FOR RESIDUE PCT C 311
source : AC4

10) chain C
residue 55
type
sequence T
description BINDING SITE FOR RESIDUE PCT C 311
source : AC4

11) chain C
residue 105
type
sequence R
description BINDING SITE FOR RESIDUE PCT C 311
source : AC4

12) chain C
residue 137
type
sequence Q
description BINDING SITE FOR RESIDUE PCT C 311
source : AC4

13) chain C
residue 55
type catalytic
sequence T
description 405
source MCSA : MCSA2

14) chain C
residue 56
type catalytic
sequence R
description 405
source MCSA : MCSA2

15) chain C
residue 85
type catalytic
sequence G
description 405
source MCSA : MCSA2

16) chain C
residue 106
type catalytic
sequence H
description 405
source MCSA : MCSA2

17) chain C
residue 135
type catalytic
sequence P
description 405
source MCSA : MCSA2

18) chain C
residue 106
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI1

19) chain C
residue 135
type BINDING
sequence P
description
source Swiss-Prot : SWS_FT_FI1

20) chain C
residue 138
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI1

21) chain C
residue 268
type BINDING
sequence P
description
source Swiss-Prot : SWS_FT_FI1

22) chain C
residue 269
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI1

23) chain C
residue 56
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI1

24) chain C
residue 85
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
source Swiss-Prot : SWS_FT_FI2

25) chain C
residue 168
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
source Swiss-Prot : SWS_FT_FI2

26) chain C
residue 230
type BINDING
sequence V
description BINDING => ECO:0000255|HAMAP-Rule:MF_00001, ECO:0000305|PubMed:3380787
source Swiss-Prot : SWS_FT_FI2


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