3ZHB
R-imine reductase from Streptomyces kanamyceticus in complex with NADP.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0050661 | molecular_function | NADP binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0050661 | molecular_function | NADP binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0016020 | cellular_component | membrane |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0050661 | molecular_function | NADP binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0016020 | cellular_component | membrane |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
D | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAP A 1307 |
Chain | Residue |
A | LEU27 |
A | VAL83 |
A | SER84 |
A | ALA88 |
A | LEU92 |
A | SER111 |
A | ILE136 |
A | ALA138 |
A | PRO140 |
A | HOH2001 |
A | GLY28 |
A | LEU29 |
A | MET30 |
A | ASN49 |
A | ARG50 |
A | THR51 |
A | LYS54 |
A | CYS82 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NAP D 1307 |
Chain | Residue |
D | LEU27 |
D | GLY28 |
D | LEU29 |
D | MET30 |
D | ASN49 |
D | ARG50 |
D | THR51 |
D | LYS54 |
D | CYS82 |
D | VAL83 |
D | SER84 |
D | ALA88 |
D | LEU92 |
D | SER111 |
D | ILE136 |
D | ALA138 |
D | PRO140 |
D | HOH2004 |
D | HOH2008 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NAP C 1307 |
Chain | Residue |
C | LEU27 |
C | GLY28 |
C | LEU29 |
C | MET30 |
C | ASN49 |
C | ARG50 |
C | THR51 |
C | LYS54 |
C | CYS82 |
C | VAL83 |
C | SER84 |
C | ALA88 |
C | LEU92 |
C | SER111 |
C | ILE136 |
C | ALA138 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NAP B 1307 |
Chain | Residue |
B | GLY26 |
B | LEU27 |
B | GLY28 |
B | MET30 |
B | ASN49 |
B | ARG50 |
B | THR51 |
B | CYS82 |
B | VAL83 |
B | SER84 |
B | ALA88 |
B | SER111 |
B | ILE136 |
B | ALA138 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 30 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGLGLMGQALaGaflgaghpttvwnr....TAAK |
Chain | Residue | Details |
A | ILE25-LYS54 |