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3QHX

Crystal Structure of Cystathionine gamma-synthase MetB (Cgs) from Mycobacterium ulcerans Agy99 bound to HEPES

Functional Information from GO Data
ChainGOidnamespacecontents
A0003962molecular_functioncystathionine gamma-synthase activity
A0004123molecular_functioncystathionine gamma-lyase activity
A0005737cellular_componentcytoplasm
A0009086biological_processmethionine biosynthetic process
A0019343biological_processcysteine biosynthetic process via cystathionine
A0019346biological_processtranssulfuration
A0030170molecular_functionpyridoxal phosphate binding
B0003962molecular_functioncystathionine gamma-synthase activity
B0004123molecular_functioncystathionine gamma-lyase activity
B0005737cellular_componentcytoplasm
B0009086biological_processmethionine biosynthetic process
B0019343biological_processcysteine biosynthetic process via cystathionine
B0019346biological_processtranssulfuration
B0030170molecular_functionpyridoxal phosphate binding
C0003962molecular_functioncystathionine gamma-synthase activity
C0004123molecular_functioncystathionine gamma-lyase activity
C0005737cellular_componentcytoplasm
C0009086biological_processmethionine biosynthetic process
C0019343biological_processcysteine biosynthetic process via cystathionine
C0019346biological_processtranssulfuration
C0030170molecular_functionpyridoxal phosphate binding
D0003962molecular_functioncystathionine gamma-synthase activity
D0004123molecular_functioncystathionine gamma-lyase activity
D0005737cellular_componentcytoplasm
D0009086biological_processmethionine biosynthetic process
D0019343biological_processcysteine biosynthetic process via cystathionine
D0019346biological_processtranssulfuration
D0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 389
ChainResidue
AARG116
ALYS120
AHIS352
AALA353
ASER354

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE EPE A 390
ChainResidue
ASER336
AMET350
AARG368
BGLU55
BTYR56
BARG58
BTHR59
BSO4389
ATYR111
AASN158
ALLP208
AGLU335

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 391
ChainResidue
AARG95
APHE122
ATRP125
BARG95
BPHE122
BTRP125

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 389
ChainResidue
AARG116
AHIS352
AEPE390
BASN237
BHOH918
BHOH1610
BHOH2003
BHOH2015

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 390
ChainResidue
BTYR111
BASN158
BLLP208
BGLU335
BSER336
BLEU337
BGLU345
BARG368
BHOH2212

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 B 391
ChainResidue
BARG313

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 389
ChainResidue
CTYR111
CASN158
CLLP208
CSER336
CLEU337
CGLU345
CARG368

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA C 390
ChainResidue
CVAL216
CVAL217
CASP247
CHOH2089
CHOH2537
DPRO245

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 D 389
ChainResidue
DTYR111
DASN158
DLLP208
DSER336
DGLU345
DARG368
DHOH1257
DHOH2224

Functional Information from PROSITE/UniProt
site_idPS00868
Number of Residues15
DetailsCYS_MET_METAB_PP Cys/Met metabolism enzymes pyridoxal-phosphate attachment site. DVvlhSTTKYIgGHS
ChainResidueDetails
AASP200-SER214

227111

PDB entries from 2024-11-06

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