eF-site ID 1ldn-G
PDB Code 1ldn
Chain G

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Title STRUCTURE OF A TERNARY COMPLEX OF AN ALLOSTERIC LACTATE DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILUS AT 2.5 ANGSTROMS RESOLUTION
Classification OXIDOREDUCTASE(CHOH(D)-NAD(A))
Compound L-LACTATE DEHYDROGENASE
Source Geobacillus stearothermophilus (Bacillus stearothermophilus) (LDH_BACST)
Sequence G:  MKNNGGARVVVIGAGFVGASYVFALMNQGIADEIVLIDAN
ESKAIGDAMDFNHGKVFAPKPVDIWHGDYDDCRDADLVVI
CAGANQKPGETRLDLVDKNIAIFRSIVESVMASGFQGLFL
VATNPVDILTYATWKFSGLPHERVIGSGTILDTARFRFLL
GEYFSVAPQNVHAYIIGEHGDTELPVWSQAYIGVMPIRKL
VESKGEEAQKDLERIFVNVRDAAYQIIEKKGATYYGIAMG
LARVTRAILHNENAILTVSAYLDGLYGERDVYIGVPAVIN
RNGIREVIEIELNDDEKNRFHHSAATLKSVLARAFT
Description


Functional site

1) chain G
residue 193
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN
source Swiss-Prot : SWS_FT_FI1

2) chain G
residue 30
type BINDING
sequence F
description BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB
source Swiss-Prot : SWS_FT_FI2

3) chain G
residue 52
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB
source Swiss-Prot : SWS_FT_FI2

4) chain G
residue 136
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB
source Swiss-Prot : SWS_FT_FI2

5) chain G
residue 57
type BINDING
sequence K
description BINDING => ECO:0000255|HAMAP-Rule:MF_00488
source Swiss-Prot : SWS_FT_FI3

6) chain G
residue 83
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_00488
source Swiss-Prot : SWS_FT_FI3

7) chain G
residue 97
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00488
source Swiss-Prot : SWS_FT_FI3

8) chain G
residue 100
type BINDING
sequence Q
description BINDING => ECO:0000255|HAMAP-Rule:MF_00488
source Swiss-Prot : SWS_FT_FI3

9) chain G
residue 119
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00488
source Swiss-Prot : SWS_FT_FI3

10) chain G
residue 138
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_00488
source Swiss-Prot : SWS_FT_FI3

11) chain G
residue 106
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN
source Swiss-Prot : SWS_FT_FI4

12) chain G
residue 166
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN
source Swiss-Prot : SWS_FT_FI4

13) chain G
residue 247
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000305|PubMed:1731077, ECO:0007744|PDB:1LDN
source Swiss-Prot : SWS_FT_FI4

14) chain G
residue 161
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB
source Swiss-Prot : SWS_FT_FI5

15) chain G
residue 183
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:1731077, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:1LDN, ECO:0007744|PDB:2LDB
source Swiss-Prot : SWS_FT_FI5

16) chain G
residue 171
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:2330370, ECO:0007744|PDB:2LDB
source Swiss-Prot : SWS_FT_FI6

17) chain G
residue 238
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000255|HAMAP-Rule:MF_00488
source Swiss-Prot : SWS_FT_FI7


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