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2VOR

Crystal Structures of Mycobacterium tuberculosis Folylpolyglutamate Synthase Complexed with ADP and AMPPCP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004326molecular_functiontetrahydrofolylpolyglutamate synthase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006761biological_processdihydrofolate biosynthetic process
A0008841molecular_functiondihydrofolate synthase activity
A0009058biological_processbiosynthetic process
A0009396biological_processfolic acid-containing compound biosynthetic process
A0016874molecular_functionligase activity
A0016881molecular_functionacid-amino acid ligase activity
A0043531molecular_functionADP binding
A0046872molecular_functionmetal ion binding
A0046901biological_processtetrahydrofolylpolyglutamate biosynthetic process
A0050897molecular_functioncobalt ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ACP A1490
ChainResidue
ATHR74
AHIS299
AASN303
AARG340
AASP353
AALA354
AHIS356
AGLY360
AALA363
AVAL474
ACO1492
AASN75
AHOH2096
AHOH2114
AGLY76
ALYS77
ATHR78
ASER79
ASER100
APRO101
AGLU176

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CO A1491
ChainResidue
AASP326
AHOH2116

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A1492
ChainResidue
ATHR78
ASER100
AGLU176
AACP1490

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A1493
ChainResidue
AHIS203
AASP205
AHOH2117
AHOH2118
AHOH2119

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CO A1494
ChainResidue
AHIS370
AASP455
AASP457
AHOH2120

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A1495
ChainResidue
ATHR74
ASER200
AASP202
AHIS203
ALYS218
AHOH2121

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A1496
ChainResidue
AARG82
AARG97
AGLY114
AALA334
ATHR336
AHOH2011
AHOH2122

Functional Information from PROSITE/UniProt
site_idPS01012
Number of Residues16
DetailsFOLYLPOLYGLU_SYNT_2 Folylpolyglutamate synthase signature 2. VVEvGMGGrwDaTnVI
ChainResidueDetails
AVAL174-ILE189

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1p3d
ChainResidueDetails
ALYS77

221371

PDB entries from 2024-06-19

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