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4M51

Crystal structure of amidohydrolase nis_0429 (ser145ala mutant) from nitratiruptor sp. sb155-2

Functional Information from GO Data
ChainGOidnamespacecontents
A0009234biological_processmenaquinone biosynthetic process
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BEZ A 501
ChainResidue
AARG89
ASER183
AHOH937
AHOH948
AHOH1132

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
AHOH975
AHOH981
AHOH1004
AHOH1005
AHOH1148
AHOH1149
AASN169
AGLN234
ATHR235
AARG236

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 503
ChainResidue
AHIS61
AHIS63
AHIS206
AASP306
AHOH962

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE EPE A 504
ChainResidue
AILE37
ALYS38
AVAL290
ALEU291
AASP292
ALEU293
AHIS327
ALYS330
AHOH607
AHOH710
AHOH924
AHOH925
AHOH996
AHOH997
AHOH1084
AHOH1099
AHOH1107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU209

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AASP306
AHIS61
AHIS63
AHIS206

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AHIS179
AGLU141

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AALA145

219869

PDB entries from 2024-05-15

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