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1VK6

Crystal structure of NADH pyrophosphatase (1790429) from Escherichia coli k12 at 2.20 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000210molecular_functionNAD+ diphosphatase activity
A0000287molecular_functionmagnesium ion binding
A0006402biological_processmRNA catabolic process
A0006734biological_processNADH metabolic process
A0006742biological_processNADP catabolic process
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0019677biological_processNAD catabolic process
A0030145molecular_functionmanganese ion binding
A0035529molecular_functionNADH pyrophosphatase activity
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0048255biological_processmRNA stabilization
A0110153molecular_functionRNA NAD-cap (NMN-forming) hydrolase activity
A0110155biological_processNAD-cap decapping
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
ACYS98
ACYS101
ACYS116
ACYS119

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 302
ChainResidue
AARG84
ATRP112
APRO125
AGLN198
AHOH377

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 303
ChainResidue
AASP2
ALEU56
AGLN58
AHOH317
AHOH367

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A 304
ChainResidue
ACYS130
AGLY159
ATRP194
AHOH388

Functional Information from PROSITE/UniProt
site_idPS00893
Number of Residues22
DetailsNUDIX_BOX Nudix box signature. GfvevgEtleqAVaREVmEEsG
ChainResidueDetails
AGLY159-GLY180

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:27428510, ECO:0007744|PDB:5IW4
ChainResidueDetails
ALYS25

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:27428510, ECO:0007744|PDB:5IW5
ChainResidueDetails
AARG69

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:27428510, ECO:0000269|PubMed:27561816, ECO:0000269|Ref.8, ECO:0007744|PDB:1VK6, ECO:0007744|PDB:2GB5, ECO:0007744|PDB:5ISY, ECO:0007744|PDB:5IW4, ECO:0007744|PDB:5IW5
ChainResidueDetails
ACYS98
ACYS101
ACYS116
ACYS119

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:27561816, ECO:0007744|PDB:5ISY
ChainResidueDetails
AGLU111

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:27428510, ECO:0000269|PubMed:27561816, ECO:0007744|PDB:5ISY, ECO:0007744|PDB:5IW4
ChainResidueDetails
ATYR124
AGLN192
AALA241

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9DCN1
ChainResidueDetails
AALA158
AGLU174
AGLU178
AGLU219

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PDB entries from 2024-11-20

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