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5IW5

Crystal structure of E. coli NudC in complex with NMN

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
B0000210molecular_functionNAD+ diphosphatase activity
B0000287molecular_functionmagnesium ion binding
B0006402biological_processmRNA catabolic process
B0006734biological_processNADH metabolic process
B0006742biological_processNADP catabolic process
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
B0019677biological_processNAD catabolic process
B0030145molecular_functionmanganese ion binding
B0035529molecular_functionNADH pyrophosphatase activity
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0048255biological_processmRNA stabilization
B0110153molecular_functionRNA NAD-cap (NMN-forming) hydrolase activity
B0110155biological_processNAD-cap decapping
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BCYS98
BCYS101
BCYS116
BCYS119

site_idAC2
Number of Residues11
Detailsbinding site for residue NMN B 302
ChainResidue
BMET201
BPRO235
BPRO236
BTHR239
BVAL240
BALA241
BARG69
BCYS130
BTRP194
BPRO197
BSER199

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
ACYS98
ACYS101
ACYS116
ACYS119

site_idAC4
Number of Residues10
Detailsbinding site for residue NMN A 302
ChainResidue
AARG69
APHE160
ATRP194
APRO197
ASER199
AMET201
APRO236
ATHR239
AALA241
AHOH425

Functional Information from PROSITE/UniProt
site_idPS00893
Number of Residues22
DetailsNUDIX_BOX Nudix box signature. GfvevgEtleqAVaREVmEEsG
ChainResidueDetails
BGLY159-GLY180

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27428510, ECO:0007744|PDB:5IW4
ChainResidueDetails
BLYS25
ALYS25

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27428510, ECO:0007744|PDB:5IW5
ChainResidueDetails
BARG69
AARG69

site_idSWS_FT_FI3
Number of Residues8
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
BCYS98
BCYS101
BCYS116
BCYS119
ACYS98
ACYS101
ACYS116
ACYS119

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27561816, ECO:0007744|PDB:5ISY
ChainResidueDetails
BGLU111
AGLU111

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:27428510, ECO:0000269|PubMed:27561816, ECO:0007744|PDB:5ISY, ECO:0007744|PDB:5IW4
ChainResidueDetails
BTYR124
BGLN192
BALA241
ATYR124
AGLN192
AALA241

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9DCN1
ChainResidueDetails
BALA158
BGLU174
BGLU178
BGLU219
AALA158
AGLU174
AGLU178
AGLU219

224004

PDB entries from 2024-08-21

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