eF-site ID 1tim-AB
PDB Code 1tim
Chain A, B

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Title STRUCTURE OF TRIOSE PHOSPHATE ISOMERASE FROM CHICKEN MUSCLE
Classification ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE)
Compound TRIOSEPHOSPHATE ISOMERASE
Source Gallus gallus (Chicken) (TPIS_CHICK)
Sequence A:  APRKFFVGGNWKMNGKRKSLGELIHTLDGAKLSADTEVVC
GAPSIYLDFARQKLDAKIGVAAQNCYKVPKGAFTGEISPA
MIKDIGAAWVILGHSERRHVFGESDELIGQKVAHALAEGL
GVIACIGEKLDEREAGITEKVVFQETKAIADNVKDWSKVV
LAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKTHVSDAVA
VQSRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFV
DIINAKH
B:  APRKFFVGGNWKMNGKRKSLGELIHTLDGAKLSADTEVVC
GAPSIYLDFARQKLDAKIGVAAQNCYKVPKGAFTGEISPA
MIKDIGAAWVILGHSERRHVFGESDELIGQKVAHALAEGL
GVIACIGEKLDEREAGITEKVVFQETKAIADNVKDWSKVV
LAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKTHVSDAVA
VQSRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFV
DIINAKH
Description


Functional site

1) chain A
residue 11
type catalytic
sequence N
description 324
source MCSA : MCSA1

2) chain A
residue 13
type catalytic
sequence K
description 324
source MCSA : MCSA1

3) chain A
residue 95
type catalytic
sequence H
description 324
source MCSA : MCSA1

4) chain A
residue 97
type catalytic
sequence E
description 324
source MCSA : MCSA1

5) chain A
residue 165
type catalytic
sequence E
description 324
source MCSA : MCSA1

6) chain A
residue 171
type catalytic
sequence G
description 324
source MCSA : MCSA1

7) chain A
residue 211
type catalytic
sequence S
description 324
source MCSA : MCSA1

8) chain B
residue 11
type catalytic
sequence N
description 324
source MCSA : MCSA2

9) chain B
residue 13
type catalytic
sequence K
description 324
source MCSA : MCSA2

10) chain B
residue 95
type catalytic
sequence H
description 324
source MCSA : MCSA2

11) chain B
residue 97
type catalytic
sequence E
description 324
source MCSA : MCSA2

12) chain B
residue 165
type catalytic
sequence E
description 324
source MCSA : MCSA2

13) chain B
residue 171
type catalytic
sequence G
description 324
source MCSA : MCSA2

14) chain B
residue 212
type catalytic
sequence V
description 324
source MCSA : MCSA2

15) chain A
residue 95
type ACT_SITE
sequence H
description Electrophile => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
source Swiss-Prot : SWS_FT_FI1

16) chain B
residue 95
type ACT_SITE
sequence H
description Electrophile => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
source Swiss-Prot : SWS_FT_FI1

17) chain A
residue 165
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
source Swiss-Prot : SWS_FT_FI2

18) chain B
residue 165
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
source Swiss-Prot : SWS_FT_FI2

19) chain A
residue 11
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
source Swiss-Prot : SWS_FT_FI3

20) chain A
residue 13
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
source Swiss-Prot : SWS_FT_FI3

21) chain B
residue 11
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
source Swiss-Prot : SWS_FT_FI3

22) chain B
residue 13
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH
source Swiss-Prot : SWS_FT_FI3

23) chain A
residue 163-173
type prosite
sequence AYEPVWAIGTG
description TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG
source prosite : PS00171


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