Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5IW4

Crystal structure of E. coli NudC in complex with NAD

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 A 500
ChainResidue
ACYS98
ACYS101
ACYS116
ACYS119

site_idAC2
Number of Residues15
Detailsbinding site for residue NAD A 501
ChainResidue
ASER199
AMET201
ATHR239
AVAL240
AALA241
AHOH602
AHOH629
BLYS25
BGLU111
BTYR124
AALA128
APHE160
AGLN192
ATRP194
APHE196

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN B 500
ChainResidue
BCYS98
BCYS101
BCYS116
BCYS119

site_idAC4
Number of Residues11
Detailsbinding site for residue NAD B 501
ChainResidue
ATYR124
AHOH626
BALA128
BCYS130
BPHE160
BTRP194
BPHE196
BMET201
BTHR239
BVAL240
BALA241

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 Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:27428510, ECO:0007744|PDB:5IW4
ChainResidueDetails
ALYS25
BLYS25

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

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
ACYS98
ACYS101
ACYS116
ACYS119
BCYS98
BCYS101
BCYS116
BCYS119

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

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
ATYR124
AGLN192
AALA241
BTYR124
BGLN192
BALA241

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

219515

PDB entries from 2024-05-08

PDB statisticsPDBj update infoContact PDBjnumon