Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2DWC

Crystal structure of Probable phosphoribosylglycinamide formyl transferase from Pyrococcus horikoshii OT3 complexed with ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006189biological_process'de novo' IMP biosynthetic process
A0009152biological_processpurine ribonucleotide biosynthetic process
A0016742molecular_functionhydroxymethyl-, formyl- and related transferase activity
A0016874molecular_functionligase activity
A0043815molecular_functionphosphoribosylglycinamide formyltransferase 2 activity
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004644molecular_functionphosphoribosylglycinamide formyltransferase activity
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006189biological_process'de novo' IMP biosynthetic process
B0009152biological_processpurine ribonucleotide biosynthetic process
B0016742molecular_functionhydroxymethyl-, formyl- and related transferase activity
B0016874molecular_functionligase activity
B0043815molecular_functionphosphoribosylglycinamide formyltransferase 2 activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 601
ChainResidue
BLYS378
BTYR382
BARG385
BHOH982
BHOH1200

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 602
ChainResidue
AARG414
ATRP420
AHOH942

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 603
ChainResidue
BTRP420
BHOH904
BHOH1004
BARG414

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 604
ChainResidue
ALYS378
ATYR382
AARG385
AHOH1074

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE ADP A 501
ChainResidue
AARG121
AHIS160
ALYS162
AGLU202
AGLU203
AHIS204
AILE205
APHE207
AGLU210
AGLN237
APHE281
AASN290
AGLU291

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ADP B 502
ChainResidue
BARG121
BHIS160
BLYS162
BGLU202
BGLU203
BHIS204
BILE205
BPHE207
BGLU210
BGLN237
BPHE281
BASN290
BGLU291
BHOH1003

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01643","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01643","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of Probable phosphoribosylglycinamide formyl transferase from Pyrococcus horikoshii OT3 complexed with ADP.","authors":["Yoshikawa S.","Arai R.","Kamo-Uchikubo T.","Shirouzu M.","Yokoyama S."]}}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ez1
ChainResidueDetails
AASP298
AARG385
ATHR299

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ez1
ChainResidueDetails
BASP298
BARG385
BTHR299

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon