eF-site ID 6szp-A PDB Code 6szp Chain A click to enlarge Title High resolution crystal structure of human DDAH-1 in complex with N-(4-Aminobutyl)-N'-(2-Methoxyethyl)guanidine Classification HYDROLASE Compound N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 Source (DDAH1_HUMAN) Sequence A:  AAFGRATHAVVRALPESLGQHALRSAKGEEVDVARAERQH QLYVGVLGSKLGLQVVELPADESLPDCVFVEDVAVVCEET ALITRPGAPSRRKEVDMMKEALEKLQLNIVEMKDENATLD GGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVP VADGLHLKSFCSMAGPNLIAIGSSESAQKALKIMQQMSDH RYDKLTVPDDIAANCIYLNIPNKGHVLLHRTPEEYPESAK VYEKLKDHMLIPVSMSELEKVDGLLTCCSVLINKK Description (1)  N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 (E.C.3.5.3.18) Functional site 1) chain A residue 30 type sequence L description binding site for residue M3B A 300 source : AC1 2) chain A residue 73 type sequence D description binding site for residue M3B A 300 source : AC1 3) chain A residue 76 type sequence F description binding site for residue M3B A 300 source : AC1 4) chain A residue 79 type sequence D description binding site for residue M3B A 300 source : AC1 5) chain A residue 98 type sequence R description binding site for residue M3B A 300 source : AC1 6) chain A residue 173 type sequence H description binding site for residue M3B A 300 source : AC1 7) chain A residue 176 type sequence S description binding site for residue M3B A 300 source : AC1 8) chain A residue 268 type sequence V description binding site for residue M3B A 300 source : AC1 9) chain A residue 269 type sequence D description binding site for residue M3B A 300 source : AC1 10) chain A residue 274 type sequence C description binding site for residue M3B A 300 source : AC1 11) chain A residue 10 type sequence F description binding site for residue GOL A 301 source : AC2 12) chain A residue 224 type sequence Y description binding site for residue GOL A 301 source : AC2 13) chain A residue 278 type sequence L description binding site for residue GOL A 301 source : AC2 14) chain A residue 159 type sequence K description binding site for residue GOL A 302 source : AC3 15) chain A residue 160 type sequence D description binding site for residue GOL A 302 source : AC3 16) chain A residue 162 type sequence A description binding site for residue GOL A 302 source : AC3 17) chain A residue 30 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI3 18) chain A residue 73 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 19) chain A residue 78 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 20) chain A residue 98 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 21) chain A residue 145 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 22) chain A residue 268 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 23) chain A residue 274 type BINDING sequence C description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 222 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000250|UniProtKB:P56965 source Swiss-Prot : SWS_FT_FI6 25) chain A residue 274 type MOD_RES sequence C description S-nitrosocysteine => ECO:0000250|UniProtKB:P56965 source Swiss-Prot : SWS_FT_FI6 26) chain A residue 173 type ACT_SITE sequence H description Proton donor => ECO:0000305|PubMed:19663506 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 274 type ACT_SITE sequence C description Nucleophile => ECO:0000269|PubMed:19663506 source Swiss-Prot : SWS_FT_FI2

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