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1G64

THE THREE-DIMENSIONAL STRUCTURE OF ATP:CORRINOID ADENOSYLTRANSFERASE FROM SALMONELLA TYPHIMURIUM. COBALAMIN/ATP TERNARY COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006779biological_processporphyrin-containing compound biosynthetic process
A0008817molecular_functioncorrinoid adenosyltransferase activity
A0009236biological_processcobalamin biosynthetic process
A0016740molecular_functiontransferase activity
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006779biological_processporphyrin-containing compound biosynthetic process
B0008817molecular_functioncorrinoid adenosyltransferase activity
B0009236biological_processcobalamin biosynthetic process
B0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 998
ChainResidue
ATHR42
AGLU128
AATP999
AHOH1331
AHOH1332

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 1001
ChainResidue
BHOH1381
BTHR242
BGLU328
BATP1000
BHOH1380

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE B12 A 800
ChainResidue
ALYS66
ATRP93
ATYR131
AARG161
AATP999
AHOH1239
BARG216
BPRO279
BHIS280
BGLN296

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP A 999
ChainResidue
AASN37
AGLY38
ALYS39
AGLY40
ALYS41
ATHR42
ATHR43
AGLU128
AARG161
AHIS182
AASP195
AB12800
AMG998
AHOH1247
AHOH1331
AHOH1332
AHOH1421
BARG251

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP B 1000
ChainResidue
AARG51
BASN237
BGLY238
BLYS239
BGLY240
BLYS241
BTHR242
BTHR243
BGLU328
BTYR331
BHIS382
BASP395
BMG1001
BHOH1214
BHOH1367
BHOH1380
BHOH1381

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 11148030
ChainResidueDetails
ATHR43
ALYS41

site_idCSA2
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 11148030
ChainResidueDetails
BTHR243
BLYS241

site_idMCSA1
Number of Residues9
DetailsM-CSA 853
ChainResidueDetails
AASN37electrostatic stabiliser
ALYS39electrostatic stabiliser
ALYS41electrostatic stabiliser
ATHR42electrostatic stabiliser, metal ligand
ATHR43electrostatic stabiliser
AARG51electrostatic stabiliser
APHE91electrostatic stabiliser
ATRP93electrostatic stabiliser
AGLU128metal ligand

site_idMCSA2
Number of Residues9
DetailsM-CSA 853
ChainResidueDetails
BASN237electrostatic stabiliser
BLYS239electrostatic stabiliser
BLYS241electrostatic stabiliser
BTHR242electrostatic stabiliser, metal ligand
BTHR243electrostatic stabiliser
BARG251electrostatic stabiliser
BPHE291electrostatic stabiliser
BTRP293electrostatic stabiliser
BGLU328metal ligand

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PDB entries from 2025-12-10

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