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5H7W

Crystal structure of 5'-nucleotidase from venom of Naja atra

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0009166biological_processnucleotide catabolic process
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0009166biological_processnucleotide catabolic process
B0016787molecular_functionhydrolase activity
B0016788molecular_functionhydrolase activity, acting on ester bonds
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00785
Number of Residues13
Details5_NUCLEOTIDASE_1 5'-nucleotidase signature 1. LtILHTnDvHArL
ChainResidueDetails
ALEU30-LEU42

site_idPS00786
Number of Residues12
Details5_NUCLEOTIDASE_2 5'-nucleotidase signature 2. YdamaLGNHEFD
ChainResidueDetails
ATYR110-ASP121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0007744|PDB:5H7W, ECO:0007744|PDB:7D0V
ChainResidueDetails
AASP37
BASN117
BHIS220
BHIS243
AHIS39
AASP85
AASN117
AHIS220
AHIS243
BASP37
BHIS39
BASP85

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P21589
ChainResidueDetails
AARG354
BPHE418
BPHE501
BASP507
AASN390
AARG395
APHE418
APHE501
AASP507
BARG354
BASN390
BARG395

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P21589
ChainResidueDetails
AHIS118
AASP121
BHIS118
BASP121

site_idSWS_FT_FI4
Number of Residues2
DetailsLIPID: GPI-anchor amidated serine => ECO:0000250|UniProtKB:P21589
ChainResidueDetails
ASER550
BSER550

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0007744|PDB:5H7W
ChainResidueDetails
AASN333
AASN347
BASN333
BASN347

218853

PDB entries from 2024-04-24

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