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3MW8

Crystal structure of an UROPORPHYRINOGEN-III SYNTHASE (Sama_3255) from SHEWANELLA AMAZONENSIS SB2B at 1.65 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004852molecular_functionuroporphyrinogen-III synthase activity
A0006779biological_processporphyrin-containing compound biosynthetic process
A0006780biological_processuroporphyrinogen III biosynthetic process
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0016829molecular_functionlyase activity
A0033014biological_processtetrapyrrole biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 301
ChainResidue
ASER179
AGLY180
AGLU181
AVAL210
AHOH399

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
AASN224
AALA225
AASP235

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
AALA143
AHOH467
AHOH512
AARG139

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
AASP173
ATRP197
AASP200
AHOH523

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
AGLN43
ATYR147
AGLU149

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 306
ChainResidue
AGLU115
AGLN116
AVAL117
ASER118
AARG141
AHOH514

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 307
ChainResidue
AILE93
ATHR94
AEDO310
AHOH340

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 308
ChainResidue
AARG166

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 309
ChainResidue
ALEU44
ALEU68
AGLN71
APRO73

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 310
ChainResidue
APRO73
ALYS74
AALA75
AEDO307

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 311
ChainResidue
AARG126
AGLY129
AGLY130
AGLU149
AHOH464

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 312
ChainResidue
AGLN43
AGLU46
AVAL123
ASER146
ATYR147
ALEU148

Functional Information from PROSITE/UniProt
site_idPS00152
Number of Residues10
DetailsATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PPLDAPASVS
ChainResidueDetails
APRO156-SER165

222624

PDB entries from 2024-07-17

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