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6III

Crystal structure of an uncharacterized protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005524molecular_functionATP binding
A0016779molecular_functionnucleotidyltransferase activity
A0018117biological_processprotein adenylylation
A0046872molecular_functionmetal ion binding
A0070733molecular_functionAMPylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue 2PN A 501
ChainResidue
AARG87
AHOH631
AHOH640
AHOH648
ALYS107
AARG170
AARG177
AASN247
AASP256
AAMP502
AMG503
AMG504

site_idAC2
Number of Residues24
Detailsbinding site for residue AMP A 502
ChainResidue
ATYR71
AGLN75
ALEU83
AGLY84
AGLY86
AARG87
ASER115
AARG116
AMET117
AGLY118
AASP119
AGLY120
AARG121
AARG159
AASN244
AASP246
AASN247
AASP256
A2PN501
AMG503
AMG504
AHOH639
AHOH685
AHOH700

site_idAC3
Number of Residues5
Detailsbinding site for residue MG A 503
ChainResidue
AASN247
AASP256
A2PN501
AAMP502
AHOH640

site_idAC4
Number of Residues3
Detailsbinding site for residue MG A 504
ChainResidue
AASP256
A2PN501
AAMP502

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00692, ECO:0000305|PubMed:30270044
ChainResidueDetails
AASP246

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q87VB1, ECO:0000255|HAMAP-Rule:MF_00692
ChainResidueDetails
AGLY84
ALYS107
AASP119
AARG170
AARG177

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00692, ECO:0000305|PubMed:30270044
ChainResidueDetails
AASN247
AASP256

219140

PDB entries from 2024-05-01

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