3N1S
Crystal structure of wild type ecHint GMP complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
| A | 0055130 | biological_process | D-alanine catabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
| B | 0055130 | biological_process | D-alanine catabolic process |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0042803 | molecular_function | protein homodimerization activity |
| E | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
| E | 0055130 | biological_process | D-alanine catabolic process |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0042803 | molecular_function | protein homodimerization activity |
| F | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
| F | 0055130 | biological_process | D-alanine catabolic process |
| I | 0000166 | molecular_function | nucleotide binding |
| I | 0003824 | molecular_function | catalytic activity |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0005829 | cellular_component | cytosol |
| I | 0016787 | molecular_function | hydrolase activity |
| I | 0042803 | molecular_function | protein homodimerization activity |
| I | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
| I | 0055130 | biological_process | D-alanine catabolic process |
| J | 0000166 | molecular_function | nucleotide binding |
| J | 0003824 | molecular_function | catalytic activity |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0005829 | cellular_component | cytosol |
| J | 0016787 | molecular_function | hydrolase activity |
| J | 0042803 | molecular_function | protein homodimerization activity |
| J | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
| J | 0055130 | biological_process | D-alanine catabolic process |
| M | 0000166 | molecular_function | nucleotide binding |
| M | 0003824 | molecular_function | catalytic activity |
| M | 0005737 | cellular_component | cytoplasm |
| M | 0005829 | cellular_component | cytosol |
| M | 0016787 | molecular_function | hydrolase activity |
| M | 0042803 | molecular_function | protein homodimerization activity |
| M | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
| M | 0055130 | biological_process | D-alanine catabolic process |
| N | 0000166 | molecular_function | nucleotide binding |
| N | 0003824 | molecular_function | catalytic activity |
| N | 0005737 | cellular_component | cytoplasm |
| N | 0005829 | cellular_component | cytosol |
| N | 0016787 | molecular_function | hydrolase activity |
| N | 0042803 | molecular_function | protein homodimerization activity |
| N | 0043530 | molecular_function | adenosine 5'-monophosphoramidase activity |
| N | 0055130 | biological_process | D-alanine catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 5GP A 201 |
| Chain | Residue |
| A | ILE6 |
| A | GLY94 |
| A | GLU96 |
| A | VAL97 |
| A | HIS101 |
| A | HIS103 |
| A | HOH123 |
| A | HOH128 |
| A | HOH188 |
| A | HOH197 |
| A | HOH732 |
| A | PHE7 |
| A | HOH1131 |
| J | HOH137 |
| A | ILE10 |
| A | PHE29 |
| A | ARG30 |
| A | ASP31 |
| A | ILE32 |
| A | LEU41 |
| A | ASN88 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 120 |
| Chain | Residue |
| A | PRO109 |
| A | LEU110 |
| A | GLY111 |
| A | HOH658 |
| B | HIS92 |
| B | GLY94 |
| B | EDO125 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 121 |
| Chain | Residue |
| A | MET113 |
| A | HOH979 |
| B | GLN35 |
| B | EDO125 |
| B | 5GP200 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 122 |
| Chain | Residue |
| A | ILE32 |
| A | PRO34 |
| A | HOH466 |
| I | PRO109 |
| I | GLY111 |
| J | LYS117 |
| J | GLY118 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE 5GP B 200 |
| Chain | Residue |
| A | EDO121 |
| B | PHE7 |
| B | PHE29 |
| B | ARG30 |
| B | ASP31 |
| B | ILE32 |
| B | LEU41 |
| B | ASN88 |
| B | GLY94 |
| B | GLU96 |
| B | VAL97 |
| B | HIS101 |
| B | HIS103 |
| B | EDO120 |
| B | HOH251 |
| B | HOH395 |
| B | HOH1114 |
| B | HOH1135 |
| B | HOH1165 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 120 |
| Chain | Residue |
| B | ILE10 |
| B | SER17 |
| B | ASP18 |
| B | PHE29 |
| B | 5GP200 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 121 |
| Chain | Residue |
| B | PRO34 |
| B | PRO37 |
| B | THR38 |
| B | HIS39 |
| B | HOH243 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 122 |
| Chain | Residue |
| A | ARG91 |
| A | HIS92 |
| B | PRO109 |
| B | LEU110 |
| B | GLY111 |
| B | HOH666 |
| B | HOH884 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 123 |
| Chain | Residue |
| B | GLN22 |
| B | ASP23 |
| B | HOH154 |
| B | HOH495 |
| B | HOH531 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 124 |
| Chain | Residue |
| B | ALA73 |
| B | GLU74 |
| B | GLY77 |
| B | ILE78 |
| B | ALA79 |
| B | GLU80 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE EDO B 125 |
| Chain | Residue |
| A | ARG84 |
| A | GLY111 |
| A | PRO112 |
| A | MET113 |
| A | EDO120 |
| A | EDO121 |
| B | ASN88 |
| B | GLY93 |
| B | GLY94 |
| B | HOH404 |
| B | HOH697 |
| site_id | BC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 5GP E 203 |
| Chain | Residue |
| E | ILE10 |
| E | PHE29 |
| E | ARG30 |
| E | ASP31 |
| E | ILE32 |
| E | LEU41 |
| E | ASN88 |
| E | GLY94 |
| E | GLU96 |
| E | VAL97 |
| E | HIS101 |
| E | HIS103 |
| E | HOH123 |
| E | HOH127 |
| E | HOH140 |
| E | HOH152 |
| E | HOH574 |
| E | HOH800 |
| E | HOH891 |
| E | HOH993 |
| E | PHE7 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO E 120 |
| Chain | Residue |
| E | PRO109 |
| E | LEU110 |
| E | GLY111 |
| F | HIS92 |
| site_id | BC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 5GP F 202 |
| Chain | Residue |
| F | PHE29 |
| F | ARG30 |
| F | ASP31 |
| F | ILE32 |
| F | LEU41 |
| F | ASN88 |
| F | GLY94 |
| F | GLN95 |
| F | GLU96 |
| F | VAL97 |
| F | HIS101 |
| F | HIS103 |
| F | HOH155 |
| F | HOH263 |
| F | HOH388 |
| F | HOH437 |
| F | HOH497 |
| F | HOH605 |
| F | HOH994 |
| F | HOH1143 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO F 120 |
| Chain | Residue |
| A | HOH459 |
| F | GLU57 |
| site_id | BC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE 5GP I 205 |
| Chain | Residue |
| I | PHE7 |
| I | PHE29 |
| I | ARG30 |
| I | ASP31 |
| I | ILE32 |
| I | LEU41 |
| I | ASN88 |
| I | GLY94 |
| I | GLN95 |
| I | GLU96 |
| I | VAL97 |
| I | HIS101 |
| I | HIS103 |
| I | EDO123 |
| I | HOH245 |
| I | HOH248 |
| I | HOH284 |
| I | HOH322 |
| I | HOH1007 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO I 120 |
| Chain | Residue |
| I | PRO34 |
| I | PRO37 |
| I | THR38 |
| I | HIS39 |
| I | HOH487 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO I 121 |
| Chain | Residue |
| I | GLU74 |
| I | GLN75 |
| I | HOH642 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO I 122 |
| Chain | Residue |
| I | GLU57 |
| I | HOH608 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO I 123 |
| Chain | Residue |
| I | GLN35 |
| I | ASN88 |
| I | 5GP205 |
| I | HOH358 |
| I | HOH430 |
| J | MET113 |
| site_id | CC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 5GP J 204 |
| Chain | Residue |
| A | HIS116 |
| J | PHE7 |
| J | ILE10 |
| J | PHE29 |
| J | ARG30 |
| J | ASP31 |
| J | ILE32 |
| J | LEU41 |
| J | ASN88 |
| J | GLY94 |
| J | GLU96 |
| J | VAL97 |
| J | HIS101 |
| J | HIS103 |
| J | HOH130 |
| J | HOH327 |
| J | HOH354 |
| J | HOH360 |
| J | HOH553 |
| J | HOH603 |
| J | HOH1154 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO J 120 |
| Chain | Residue |
| J | GLU4 |
| J | SER8 |
| J | ARG12 |
| J | ASN45 |
| J | HOH879 |
| site_id | CC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO J 121 |
| Chain | Residue |
| B | LEU119 |
| J | PRO34 |
| J | GLN35 |
| J | ALA36 |
| J | PRO37 |
| J | ARG108 |
| J | HOH573 |
| N | GLU3 |
| site_id | CC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 5GP M 207 |
| Chain | Residue |
| M | ILE6 |
| M | PHE29 |
| M | ARG30 |
| M | ASP31 |
| M | ILE32 |
| M | LEU41 |
| M | ASN88 |
| M | GLY94 |
| M | GLN95 |
| M | GLU96 |
| M | VAL97 |
| M | HIS101 |
| M | HIS103 |
| M | HOH130 |
| M | HOH313 |
| M | HOH431 |
| M | HOH594 |
| M | HOH829 |
| M | HOH935 |
| M | HOH966 |
| M | HOH975 |
| site_id | CC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO M 120 |
| Chain | Residue |
| F | LYS117 |
| M | PRO109 |
| M | LEU110 |
| M | GLY111 |
| M | HOH539 |
| N | HIS92 |
| site_id | CC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO M 121 |
| Chain | Residue |
| M | GLN75 |
| M | HOH389 |
| M | HOH926 |
| site_id | CC9 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE 5GP N 206 |
| Chain | Residue |
| F | HIS116 |
| N | ILE6 |
| N | PHE7 |
| N | ILE10 |
| N | PHE29 |
| N | ARG30 |
| N | ASP31 |
| N | ILE32 |
| N | LEU41 |
| N | ASN88 |
| N | GLY94 |
| N | GLN95 |
| N | GLU96 |
| N | VAL97 |
| N | HIS101 |
| N | HIS103 |
| N | EDO121 |
| N | EDO123 |
| N | HOH132 |
| N | HOH140 |
| N | HOH147 |
| N | HOH312 |
| N | HOH391 |
| N | HOH515 |
| N | HOH554 |
| N | HOH1163 |
| N | HOH1167 |
| site_id | DC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO N 120 |
| Chain | Residue |
| N | ARG12 |
| N | ARG13 |
| N | GLU14 |
| site_id | DC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO N 121 |
| Chain | Residue |
| F | LYS117 |
| F | HOH518 |
| M | ARG84 |
| M | GLY111 |
| M | MET113 |
| N | ASN88 |
| N | GLY93 |
| N | GLY94 |
| N | 5GP206 |
| site_id | DC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO N 122 |
| Chain | Residue |
| N | ARG12 |
| N | ASN45 |
| N | HOH390 |
| N | HOH421 |
| site_id | DC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO N 123 |
| Chain | Residue |
| J | MET1 |
| N | SER17 |
| N | ASP18 |
| N | ARG30 |
| N | 5GP206 |
| N | HOH391 |
| site_id | DC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO N 124 |
| Chain | Residue |
| B | GLU80 |
| B | ASP81 |
| N | TYR21 |
| N | GLN22 |
| N | HOH1111 |
| site_id | DC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO N 125 |
| Chain | Residue |
| N | ASP81 |
Functional Information from PROSITE/UniProt
| site_id | PS00892 |
| Number of Residues | 19 |
| Details | HIT_1 HIT domain signature. NtnrhGgQeVyHIHMHLLG |
| Chain | Residue | Details |
| A | ASN88-GLY106 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Tele-AMP-histidine intermediate => ECO:0000269|PubMed:15703176, ECO:0000269|PubMed:20934431 |
| Chain | Residue | Details |
| A | HIS101 | |
| B | HIS101 | |
| E | HIS101 | |
| F | HIS101 | |
| I | HIS101 | |
| J | HIS101 | |
| M | HIS101 | |
| N | HIS101 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20934431, ECO:0007744|PDB:3N1S |
| Chain | Residue | Details |
| A | ARG30 | |
| E | ASN88 | |
| E | GLU96 | |
| E | HIS101 | |
| F | ARG30 | |
| F | ASN88 | |
| F | GLU96 | |
| F | HIS101 | |
| I | ARG30 | |
| I | ASN88 | |
| I | GLU96 | |
| A | ASN88 | |
| I | HIS101 | |
| J | ARG30 | |
| J | ASN88 | |
| J | GLU96 | |
| J | HIS101 | |
| M | ARG30 | |
| M | ASN88 | |
| M | GLU96 | |
| M | HIS101 | |
| N | ARG30 | |
| A | GLU96 | |
| N | ASN88 | |
| N | GLU96 | |
| N | HIS101 | |
| A | HIS101 | |
| B | ARG30 | |
| B | ASN88 | |
| B | GLU96 | |
| B | HIS101 | |
| E | ARG30 |
