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1FKX

MURINE ADENOSINE DEAMINASE (D296A)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000255biological_processallantoin metabolic process
A0001666biological_processresponse to hypoxia
A0001701biological_processin utero embryonic development
A0001821biological_processhistamine secretion
A0001829biological_processtrophectodermal cell differentiation
A0001883molecular_functionpurine nucleoside binding
A0001889biological_processliver development
A0001890biological_processplacenta development
A0002314biological_processgerminal center B cell differentiation
A0002467biological_processgerminal center formation
A0002636biological_processpositive regulation of germinal center formation
A0002686biological_processnegative regulation of leukocyte migration
A0002901biological_processmature B cell apoptotic process
A0002906biological_processnegative regulation of mature B cell apoptotic process
A0004000molecular_functionadenosine deaminase activity
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006154biological_processadenosine catabolic process
A0006157biological_processdeoxyadenosine catabolic process
A0006196biological_processAMP catabolic process
A0006915biological_processapoptotic process
A0006939biological_processsmooth muscle contraction
A0007155biological_processcell adhesion
A0008270molecular_functionzinc ion binding
A0009117biological_processnucleotide metabolic process
A0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
A0009897cellular_componentexternal side of plasma membrane
A0009986cellular_componentcell surface
A0010035biological_processresponse to inorganic substance
A0010460biological_processpositive regulation of heart rate
A0014074biological_processresponse to purine-containing compound
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019239molecular_functiondeaminase activity
A0019722biological_processcalcium-mediated signaling
A0030217biological_processT cell differentiation
A0030324biological_processlung development
A0030890biological_processpositive regulation of B cell proliferation
A0031410cellular_componentcytoplasmic vesicle
A0032261biological_processpurine nucleotide salvage
A0032263biological_processGMP salvage
A0032264biological_processIMP salvage
A0032839cellular_componentdendrite cytoplasm
A0033077biological_processT cell differentiation in thymus
A0033081biological_processregulation of T cell differentiation in thymus
A0033089biological_processpositive regulation of T cell differentiation in thymus
A0033197biological_processresponse to vitamin E
A0033632biological_processregulation of cell-cell adhesion mediated by integrin
A0042100biological_processB cell proliferation
A0042110biological_processT cell activation
A0042323biological_processnegative regulation of circadian sleep/wake cycle, non-REM sleep
A0043025cellular_componentneuronal cell body
A0043066biological_processnegative regulation of apoptotic process
A0043084biological_processpenile erection
A0043103biological_processhypoxanthine salvage
A0043605biological_processamide catabolic process
A0044209biological_processAMP salvage
A0045580biological_processregulation of T cell differentiation
A0045582biological_processpositive regulation of T cell differentiation
A0045987biological_processpositive regulation of smooth muscle contraction
A0046059biological_processdAMP catabolic process
A0046061biological_processdATP catabolic process
A0046085biological_processadenosine metabolic process
A0046101biological_processhypoxanthine biosynthetic process
A0046103biological_processinosine biosynthetic process
A0046111biological_processxanthine biosynthetic process
A0046632biological_processalpha-beta T cell differentiation
A0046638biological_processpositive regulation of alpha-beta T cell differentiation
A0046872molecular_functionmetal ion binding
A0046936molecular_function2'-deoxyadenosine deaminase activity
A0048286biological_processlung alveolus development
A0048541biological_processPeyer's patch development
A0048566biological_processembryonic digestive tract development
A0050728biological_processnegative regulation of inflammatory response
A0050850biological_processpositive regulation of calcium-mediated signaling
A0050852biological_processT cell receptor signaling pathway
A0050862biological_processpositive regulation of T cell receptor signaling pathway
A0050870biological_processpositive regulation of T cell activation
A0050900biological_processleukocyte migration
A0060169biological_processnegative regulation of adenosine receptor signaling pathway
A0060205cellular_componentcytoplasmic vesicle lumen
A0060407biological_processnegative regulation of penile erection
A0070161cellular_componentanchoring junction
A0070242biological_processthymocyte apoptotic process
A0070244biological_processnegative regulation of thymocyte apoptotic process
A0070254biological_processmucus secretion
A0070256biological_processnegative regulation of mucus secretion
A0140928biological_processinhibition of non-skeletal tissue mineralization
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
AHIS15
AHIS17
AHIS214
AASP295
APRH353

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PRH A 353
ChainResidue
ALEU106
AMET155
AGLY184
AHIS214
AGLU217
AHIS238
AASP295
AZN400
AHOH437
AHIS17
AASP19
APHE61
APHE65

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:8634299, ECO:0000305|PubMed:9622483
ChainResidueDetails
AGLU217

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA
ChainResidueDetails
AHIS15
AHIS17
AHIS214
AASP295

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4L, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1FKX
ChainResidueDetails
AASP19

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483, ECO:0007744|PDB:1A4M, ECO:0007744|PDB:1FKX, ECO:0007744|PDB:1UIO, ECO:0007744|PDB:1UIP, ECO:0007744|PDB:2ADA
ChainResidueDetails
AGLY184

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:8942668, ECO:0007744|PDB:1FKW, ECO:0007744|PDB:1UIP
ChainResidueDetails
AALA296

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813
ChainResidueDetails
ALEU58
ALEU62

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000269|PubMed:8942668, ECO:0000269|PubMed:9622483
ChainResidueDetails
AHIS238

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00813
ChainResidueDetails
ALYS54
ALYS232

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 376
ChainResidueDetails
AHIS15metal ligand
AHIS17metal ligand
AHIS214metal ligand
AGLU217proton shuttle (general acid/base)
AHIS238proton shuttle (general acid/base)
AASP295metal ligand, steric role

218853

PDB entries from 2024-04-24

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