eF-site ID 2v30-B
PDB Code 2v30
Chain B

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Title Human orotidine 5'-phosphate decarboxylase domain of uridine monophospate synthetase (UMPS) in complex with its product UMP.
Classification LYASE
Compound OROTIDINE 5'-PHOSPHATE DECARBOXYLASE
Source Homo sapiens (Human) (PYR5_HUMAN)
Sequence B:  MELSFGARAELPRIHPVASKLLRLMQKKETNLCLSADVSL
ARELLQLADALGPSICMLKTHVDILNDFTLDVMKELITLA
KCHEFLIFEDRKFADIGNTVKKQYEGGIFKIASWADLVNA
HVVPGSGVVKGLQEVGLPLHRGCLLIAEMSSTGSLATGDY
TRAAVRMAEEHSEFVVGFISGSRVSMKPEFLHLTPGVQLE
AGGDNLGQQYNSPQEVIGKRGSDIIIVGRGIISAADRLEA
AEMYRKAAWEAYLSRL
Description


Functional site

1) chain B
residue 317
type
sequence D
description BINDING SITE FOR RESIDUE U5P A1480
source : AC1

2) chain B
residue 318
type
sequence I
description BINDING SITE FOR RESIDUE U5P A1480
source : AC1

3) chain B
residue 321
type
sequence T
description BINDING SITE FOR RESIDUE U5P A1480
source : AC1

4) chain B
residue 257
type
sequence S
description BINDING SITE FOR RESIDUE U5P B1479
source : AC2

5) chain B
residue 259
type
sequence D
description BINDING SITE FOR RESIDUE U5P B1479
source : AC2

6) chain B
residue 281
type
sequence K
description BINDING SITE FOR RESIDUE U5P B1479
source : AC2

7) chain B
residue 283
type
sequence H
description BINDING SITE FOR RESIDUE U5P B1479
source : AC2

8) chain B
residue 312
type
sequence D
description BINDING SITE FOR RESIDUE U5P B1479
source : AC2

9) chain B
residue 314
type
sequence K
description BINDING SITE FOR RESIDUE U5P B1479
source : AC2

10) chain B
residue 371
type
sequence M
description BINDING SITE FOR RESIDUE U5P B1479
source : AC2

11) chain B
residue 372
type
sequence S
description BINDING SITE FOR RESIDUE U5P B1479
source : AC2

12) chain B
residue 417
type
sequence P
description BINDING SITE FOR RESIDUE U5P B1479
source : AC2

13) chain B
residue 430
type
sequence Q
description BINDING SITE FOR RESIDUE U5P B1479
source : AC2

14) chain B
residue 432
type
sequence Y
description BINDING SITE FOR RESIDUE U5P B1479
source : AC2

15) chain B
residue 450
type
sequence G
description BINDING SITE FOR RESIDUE U5P B1479
source : AC2

16) chain B
residue 451
type
sequence R
description BINDING SITE FOR RESIDUE U5P B1479
source : AC2

17) chain B
residue 312
type ACT_SITE
sequence D
description For OMPdecase activity => ECO:0000269|PubMed:18184586
source Swiss-Prot : SWS_FT_FI1

18) chain B
residue 314
type ACT_SITE
sequence K
description For OMPdecase activity => ECO:0000269|PubMed:18184586
source Swiss-Prot : SWS_FT_FI1

19) chain B
residue 317
type ACT_SITE
sequence D
description For OMPdecase activity => ECO:0000269|PubMed:18184586
source Swiss-Prot : SWS_FT_FI1

20) chain B
residue 281
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCL
source Swiss-Prot : SWS_FT_FI4

21) chain B
residue 314
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCL
source Swiss-Prot : SWS_FT_FI4

22) chain B
residue 257
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD
source Swiss-Prot : SWS_FT_FI2

23) chain B
residue 317
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD
source Swiss-Prot : SWS_FT_FI2

24) chain B
residue 321
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD
source Swiss-Prot : SWS_FT_FI2

25) chain B
residue 259
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD, ECO:0007744|PDB:2QCH
source Swiss-Prot : SWS_FT_FI3

26) chain B
residue 372
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD, ECO:0007744|PDB:2QCH
source Swiss-Prot : SWS_FT_FI3

27) chain B
residue 430
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD, ECO:0007744|PDB:2QCH
source Swiss-Prot : SWS_FT_FI3

28) chain B
residue 450
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:18184586, ECO:0007744|PDB:2QCD, ECO:0007744|PDB:2QCH
source Swiss-Prot : SWS_FT_FI3


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