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4M9D

The Crystal structure of an adenylosuccinate synthetase from Bacillus anthracis str. Ames Ancestor in complex with AMP.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004019molecular_functionadenylosuccinate synthase activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0006164biological_processpurine nucleotide biosynthetic process
A0016874molecular_functionligase activity
A0044208biological_process'de novo' AMP biosynthetic process
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004019molecular_functionadenylosuccinate synthase activity
B0005525molecular_functionGTP binding
B0005737cellular_componentcytoplasm
B0006164biological_processpurine nucleotide biosynthetic process
B0016874molecular_functionligase activity
B0044208biological_process'de novo' AMP biosynthetic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE AMP A 501
ChainResidue
ATRP11
ATHR238
AVAL272
AGLY273
AEDO503
AHOH607
AHOH626
AHOH657
AHOH660
AHOH782
AHOH783
AGLY12
AHOH785
BARG142
AASN38
AGLY126
ATHR127
ATHR128
AGLN223
ALEU227
AVAL237

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MLI A 502
ChainResidue
AGLY12
AASP13
AGLU14
AGLY15
ALYS16
AGLY17
AHIS41
AEDO503
AHOH652
AHOH825

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 503
ChainResidue
AGLY12
AASP13
AGLY40
AARG304
AAMP501
AMLI502

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 504
ChainResidue
ATHR128
ALYS130

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FMT A 505
ChainResidue
AGLU355
APRO357
AALA358
AASN359
BASN100

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE AMP B 501
ChainResidue
AARG142
BTRP11
BASP13
BASN38
BGLY126
BTHR127
BTHR128
BGLN223
BLEU227
BVAL237
BTHR238
BVAL272
BGLY273
BMLI503
BFMT508
BHOH620
BHOH629
BHOH632
BHOH641
BHOH669
BHOH672
BHOH680
BHOH808
BHOH869

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MLI B 502
ChainResidue
AVAL261
AGLY322
ATHR324
BGLY254
BPRO255
BALA256
BLYS257
BHOH784

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MLI B 503
ChainResidue
BASN38
BTHR128
BLYS130
BAMP501
BEDO506
BHOH749
BHOH769
BHOH783
BHOH905

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 504
ChainResidue
ALYS257
BARG318
BGLY322
BLEU323

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 505
ChainResidue
BGLN198
BVAL200

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 506
ChainResidue
BGLY297
BTHR298
BTHR299
BTHR300
BMLI503
BHOH883

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 507
ChainResidue
BHOH904
BGLU25
BHIS26

site_idBC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FMT B 508
ChainResidue
BLYS16
BALA39
BGLY40
BALA222
BGLN223
BAMP501
BPO4510
BHOH869

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT B 509
ChainResidue
BGLY126
BVAL272

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 510
ChainResidue
BASP13
BGLU14
BGLY15
BLYS16
BGLY17
BGLY40
BFMT508

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues11
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pi.AGgVTVGTG
ChainResidueDetails
APRO242-GLY252

site_idPS00513
Number of Residues12
DetailsADENYLOSUCCIN_SYN_2 Adenylosuccinate synthetase active site. GIGPaYmdKaaR
ChainResidueDetails
AGLY131-ARG142

site_idPS01266
Number of Residues8
DetailsADENYLOSUCCIN_SYN_1 Adenylosuccinate synthetase GTP-binding site. QWGDEGKG
ChainResidueDetails
AGLN10-GLY17

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00011
ChainResidueDetails
AASP13
BASP13

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00011
ChainResidueDetails
AHIS41
BHIS41

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00011
ChainResidueDetails
AGLY12
BASP13
BGLY40
BARG142
BTHR298
BARG304
BSER330
BSER412
AASP13
AGLY40
AARG142
ATHR298
AARG304
ASER330
ASER412
BGLY12

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00011
ChainResidueDetails
AASN38
BARG302
ATHR128
AGLN223
ATHR238
AARG302
BASN38
BTHR128
BGLN223
BTHR238

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PDB entries from 2024-07-17

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