eF-site ID 6n4j-AB
PDB Code 6n4j
Chain A, B

click to enlarge
Title Ti(III)citrate-reduced, nucleotide-free form of the nitrogenase Fe-protein from A. vinelandii
Classification OXIDOREDUCTASE
Compound Nitrogenase iron protein 1
Source ORGANISM_SCIENTIFIC: Azotobacter vinelandii;
Sequence A:  AMRQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDP
KADSTRLILHSKAQNTIMEMAAEAGTVEDLELEDVLKAGY
GGVKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLD
FVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYA
ANNISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALA
NKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEY
RALARKVVDNKLLVIPNPITMDELEELLMEFGIMEVEDES
IVGKTAEEV
B:  AMRQCAIYGKGGIGKSTTTQNLVAALAEMGKKVMIVGCDP
KADSTRLILHSKAQNTIMEMAAEAGTVEDLELEDVLKAGY
GGVKCVESGGPEPGVGCAGRGVITAINFLEEEGAYEDDLD
FVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYA
ANNISKGIVKYANSGSVRLGGLICNSRNTDREDELIIALA
NKLGTQMIHFVPRDNVVQRAEIRRMTVIEYDPKAKQADEY
RALARKVVDNKLLVIPNPITMDELEELLMEFGIMEVEDES
IVGKTA
Description


Functional site

1) chain A
residue 97
type
sequence C
description binding site for residue SF4 A 301
source : AC1

2) chain A
residue 98
type
sequence A
description binding site for residue SF4 A 301
source : AC1

3) chain A
residue 132
type
sequence C
description binding site for residue SF4 A 301
source : AC1

4) chain A
residue 134
type
sequence G
description binding site for residue SF4 A 301
source : AC1

5) chain B
residue 97
type
sequence C
description binding site for residue SF4 A 301
source : AC1

6) chain B
residue 132
type
sequence C
description binding site for residue SF4 A 301
source : AC1

7) chain B
residue 134
type
sequence G
description binding site for residue SF4 A 301
source : AC1

8) chain A
residue 125-138
type prosite
sequence DVLGDVVCGGFAMP
description NIFH_FRXC_2 NifH/frxC family signature 2. DvLGDVVCGGFAmP
source prosite : PS00692

9) chain A
residue 87-99
type prosite
sequence ESGGPEPGVGCAG
description NIFH_FRXC_1 NifH/frxC family signature 1. EsGGPepGvGCAG
source prosite : PS00746

10) chain A
residue 10
type catalytic
sequence K
description 212
source MCSA : MCSA1

11) chain A
residue 15
type catalytic
sequence K
description 212
source MCSA : MCSA1

12) chain A
residue 41
type catalytic
sequence K
description 212
source MCSA : MCSA1

13) chain A
residue 129
type catalytic
sequence D
description 212
source MCSA : MCSA1

14) chain B
residue 10
type catalytic
sequence K
description 212
source MCSA : MCSA2

15) chain B
residue 15
type catalytic
sequence K
description 212
source MCSA : MCSA2

16) chain B
residue 41
type catalytic
sequence K
description 212
source MCSA : MCSA2

17) chain B
residue 129
type catalytic
sequence D
description 212
source MCSA : MCSA2

18) chain A
residue 132
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI1

19) chain B
residue 9
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI1

20) chain B
residue 97
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI1

21) chain B
residue 132
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI1

22) chain A
residue 9
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI1

23) chain A
residue 97
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI1

24) chain A
residue 100
type MOD_RES
sequence R
description ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

25) chain B
residue 100
type MOD_RES
sequence R
description ADP-ribosylarginine; by dinitrogenase reductase ADP-ribosyltransferase => ECO:0000250
source Swiss-Prot : SWS_FT_FI2


Display surface

Download
Links