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

click to enlarge
Title METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE PYROCOCCUS FURIOSUS
Classification AMINOPEPTIDASE
Compound METHIONINE AMINOPEPTIDASE
Source ORGANISM_SCIENTIFIC: Pyrococcus furiosus;
Sequence A:  MDTEKLMKAGEIAKKVREKAIKLARPGMLLLELAESIEKM
IMELGGKPAFPVNLSINEIAAHYTPYKGDTTVLKEGDYLK
IDVGVHIDGFIADTAVTVRVGMEEDELMEAAKEALNAAIS
VARAGVEIKELGKAIENEIRKRGFKPIVNLSGHKIERYKL
HAGISIPNIYRPHDNYVLKEGDVFAIEPFATIGAGQVIEV
PPTLIYMYVRDVPVRVAQARFLLAKIKREYGTLPFAYRWL
QNDMPEGQLKLALKTLEKAGAIYGYPVLKEIRNGIVAQFE
HTIIVEKDSVIVTTE
Description


Functional site

1) chain A
residue 82
type
sequence D
description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN A.
source : ACA

2) chain A
residue 93
type
sequence D
description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN A.
source : ACA

3) chain A
residue 153
type
sequence H
description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN A.
source : ACA

4) chain A
residue 187
type
sequence E
description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN A.
source : ACA

5) chain A
residue 280
type
sequence E
description SIDE CHAINS OF FIVE AMINO ACID RESIDUES ASP 82, ASP 93, HIS 153, GLU 187, GLU 280, AND TWO COBALT IONS FORM AN ACTIVE SITE OF MOLECULE IN CHAIN A.
source : ACA

6) chain A
residue 93
type
sequence D
description BINDING SITE FOR RESIDUE CO A 296
source : AC1

7) chain A
residue 153
type
sequence H
description BINDING SITE FOR RESIDUE CO A 296
source : AC1

8) chain A
residue 187
type
sequence E
description BINDING SITE FOR RESIDUE CO A 296
source : AC1

9) chain A
residue 280
type
sequence E
description BINDING SITE FOR RESIDUE CO A 296
source : AC1

10) chain A
residue 82
type
sequence D
description BINDING SITE FOR RESIDUE CO A 297
source : AC2

11) chain A
residue 93
type
sequence D
description BINDING SITE FOR RESIDUE CO A 297
source : AC2

12) chain A
residue 280
type
sequence E
description BINDING SITE FOR RESIDUE CO A 297
source : AC2

13) chain A
residue 82
type catalytic
sequence D
description 917
source MCSA : MCSA1

14) chain A
residue 93
type catalytic
sequence D
description 917
source MCSA : MCSA1

15) chain A
residue 153
type catalytic
sequence H
description 917
source MCSA : MCSA1

16) chain A
residue 161
type catalytic
sequence H
description 917
source MCSA : MCSA1

17) chain A
residue 187
type catalytic
sequence E
description 917
source MCSA : MCSA1

18) chain A
residue 280
type catalytic
sequence E
description 917
source MCSA : MCSA1

19) chain A
residue 62
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_01975
source Swiss-Prot : SWS_FT_FI1

20) chain A
residue 82
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

21) chain A
residue 93
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

22) chain A
residue 153
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

23) chain A
residue 161
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

24) chain A
residue 187
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

25) chain A
residue 280
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 77-93
type prosite
sequence DYLKIDVGVHIDGFIAD
description MAP_2 Methionine aminopeptidase subfamily 2 signature. DYlKIDvGvHIDGfiaD
source prosite : PS01202


Display surface

Download
Links