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3FCC

CRYSTAL STRUCTURE OF DLTA PROTEIN IN COMPLEX WITH ATP and MAGNESIUM

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0016874molecular_functionligase activity
A0047473molecular_functionD-alanine [D-alanyl carrier protein] ligase activity
A0070395biological_processlipoteichoic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 710
ChainResidue
AATP711
AHOH791
AHOH792
AHOH793
AHOH794

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ATP A 711
ChainResidue
AGLU271
AVAL272
AASN292
ATHR293
ATYR294
AGLY295
ATHR297
AASP383
ATYR394
AARG397
ALYS492
AMG710
AHOH791
AHOH792
AHOH793
AHOH806
AHOH895
ATHR152
ASER153
APHE196
AGLY270

Functional Information from PROSITE/UniProt
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. IIYTSGSTGnPK
ChainResidueDetails
AILE149-LYS160

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00593, ECO:0000269|PubMed:19324056, ECO:0007744|PDB:3FCC, ECO:0007744|PDB:3FCE
ChainResidueDetails
ATHR152

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00593, ECO:0000269|PubMed:18847223, ECO:0007744|PDB:3DHV
ChainResidueDetails
AASP197
AVAL301
ALYS492

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00593, ECO:0000269|PubMed:18847223, ECO:0000269|PubMed:19324056, ECO:0007744|PDB:3FCC, ECO:0007744|PDB:3FCE
ChainResidueDetails
AASN292
AASP383
ATYR394

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PDB entries from 2025-06-18

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